Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1
Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on me...
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| Published in | The EMBO journal Vol. 29; no. 20; pp. 3571 - 3589 |
|---|---|
| Main Authors | , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
20.10.2010
Nature Publishing Group UK Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with
in vitro
vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in
Caenorhabditis elegans
, αS binds to mitochondria and leads to mitochondrial fragmentation. In
C. elegans
age‐dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA‐mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ‐1 but not the PD‐associated mutations PINK1 G309D and parkin Δ1–79 or by DJ‐1 C106A.
This study demonstrates that α‐synuclein, which is implicated in the pathogenesis of Parkinson's disease, regulates mitochondrial dynamics by direct inhibition of membrane fusion. |
|---|---|
| AbstractList | Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with
in vitro
vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in
Caenorhabditis elegans
, αS binds to mitochondria and leads to mitochondrial fragmentation. In
C. elegans
age‐dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA‐mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ‐1 but not the PD‐associated mutations PINK1 G309D and parkin Δ1–79 or by DJ‐1 C106A.
This study demonstrates that α‐synuclein, which is implicated in the pathogenesis of Parkinson's disease, regulates mitochondrial dynamics by direct inhibition of membrane fusion. This study demonstrates that α-synuclein, which is implicated in the pathogenesis of Parkinson's disease, regulates mitochondrial dynamics by direct inhibition of membrane fusion. Aggregation of α-synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in Caenorhabditis elegans , αS binds to mitochondria and leads to mitochondrial fragmentation. In C. elegans age-dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA-mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ-1 but not the PD-associated mutations PINK1 G309D and parkin Δ1–79 or by DJ-1 C106A. Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in Caenorhabditis elegans, αS binds to mitochondria and leads to mitochondrial fragmentation. In C. elegans age‐dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA‐mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ‐1 but not the PD‐associated mutations PINK1 G309D and parkin Δ1–79 or by DJ‐1 C106A. This study demonstrates that α‐synuclein, which is implicated in the pathogenesis of Parkinson's disease, regulates mitochondrial dynamics by direct inhibition of membrane fusion. Aggregation of alpha -synuclein ( alpha S) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of alpha S is largely unknown. We demonstrate with in vitro vesicle fusion experiments that alpha S has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in Caenorhabditis elegans, alpha S binds to mitochondria and leads to mitochondrial fragmentation. In C. elegans age-dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous alpha S. In contrast, siRNA-mediated downregulation of alpha S results in elongated mitochondria in cell culture. alpha S can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, alpha S prevents fusion of differently labelled mitochondrial populations. Thus, alpha S inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of alpha S is rescued by coexpression of PINK1, parkin or DJ-1 but not the PD-associated mutations PINK1 G309D and parkin Delta 1-79 or by DJ-1 C106A. Aggregation of α-synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in Caenorhabditis elegans, αS binds to mitochondria and leads to mitochondrial fragmentation. In C. elegans age-dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA-mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ-1 but not the PD-associated mutations PINK1 G309D and parkin Δ1-79 or by DJ-1 C106A. Aggregation of α-synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in Caenorhabditis elegans, αS binds to mitochondria and leads to mitochondrial fragmentation. In C. elegans age-dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA-mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ-1 but not the PD-associated mutations PINK1 G309D and parkin Δ1-79 or by DJ-1 C106A.Aggregation of α-synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on membrane fusion. Upon increased expression in cultured cells and in Caenorhabditis elegans, αS binds to mitochondria and leads to mitochondrial fragmentation. In C. elegans age-dependent fragmentation of mitochondria is enhanced and shifted to an earlier time point upon expression of exogenous αS. In contrast, siRNA-mediated downregulation of αS results in elongated mitochondria in cell culture. αS can act independently of mitochondrial fusion and fission proteins in shifting the dynamic morphologic equilibrium of mitochondria towards reduced fusion. Upon cellular fusion, αS prevents fusion of differently labelled mitochondrial populations. Thus, αS inhibits fusion due to its unique membrane interaction. Finally, mitochondrial fragmentation induced by expression of αS is rescued by coexpression of PINK1, parkin or DJ-1 but not the PD-associated mutations PINK1 G309D and parkin Δ1-79 or by DJ-1 C106A. |
| Author | Bartels, Tim Beyer, Klaus Exner, Nicole Brunner, Bettina Haass, Christian Nuscher, Brigitte Eimer, Stefan Wender, Nora Lutz, Anne Kathrin Giese, Armin Winklhofer, Konstanze F Hegermann, Jan Kamp, Frits |
| Author_xml | – sequence: 1 givenname: Frits surname: Kamp fullname: Kamp, Frits email: fkamp@med.uni-muenchen.de organization: DZNE-German Center for Neurodegenerative Diseases, Munich, Germany – sequence: 2 givenname: Nicole surname: Exner fullname: Exner, Nicole organization: DZNE-German Center for Neurodegenerative Diseases, Munich, Germany – sequence: 3 givenname: Anne Kathrin surname: Lutz fullname: Lutz, Anne Kathrin organization: Adolf-Butenandt-Institute, Neurobiochemistry, Ludwig-Maximilians-University, Munich, Germany – sequence: 4 givenname: Nora surname: Wender fullname: Wender, Nora organization: European Neuroscience Institute Goettingen and DFG Research Center for Molecular Physiology of the Brain (CMPB), Goettingen, Germany – sequence: 5 givenname: Jan surname: Hegermann fullname: Hegermann, Jan organization: European Neuroscience Institute Goettingen and DFG Research Center for Molecular Physiology of the Brain (CMPB), Goettingen, Germany – sequence: 6 givenname: Bettina surname: Brunner fullname: Brunner, Bettina organization: DZNE-German Center for Neurodegenerative Diseases, Munich, Germany – sequence: 7 givenname: Brigitte surname: Nuscher fullname: Nuscher, Brigitte organization: DZNE-German Center for Neurodegenerative Diseases, Munich, Germany – sequence: 8 givenname: Tim surname: Bartels fullname: Bartels, Tim organization: Adolf-Butenandt-Institute, Biochemistry, Ludwig-Maximilians-University, Munich, Germany – sequence: 9 givenname: Armin surname: Giese fullname: Giese, Armin organization: Center for Neuropathology and Prion Research, Ludwig-Maximilians-University, Munich, Germany – sequence: 10 givenname: Klaus surname: Beyer fullname: Beyer, Klaus organization: Adolf-Butenandt-Institute, Biochemistry, Ludwig-Maximilians-University, Munich, Germany – sequence: 11 givenname: Stefan surname: Eimer fullname: Eimer, Stefan organization: European Neuroscience Institute Goettingen and DFG Research Center for Molecular Physiology of the Brain (CMPB), Goettingen, Germany – sequence: 12 givenname: Konstanze F surname: Winklhofer fullname: Winklhofer, Konstanze F organization: Adolf-Butenandt-Institute, Neurobiochemistry, Ludwig-Maximilians-University, Munich, Germany – sequence: 13 givenname: Christian surname: Haass fullname: Haass, Christian email: fkamp@med.uni-muenchen.de organization: DZNE-German Center for Neurodegenerative Diseases, Munich, Germany |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20842103$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1016/S0092-8674(00)81404-X 10.1083/jcb.200507087 10.1046/j.0014-2956.2001.02649.x 10.1529/biophysj.105.069617 10.1097/WNR.0b013e3282f03db4 10.1007/978-1-59745-365-3_1 10.1016/j.neuron.2009.12.023 10.1111/j.1471-4159.2004.02854.x 10.1177/002215540405200101 10.1016/0896-6273(95)90302-X 10.1016/j.brainres.2004.04.018 10.1074/jbc.M808591200 10.2144/04363ST01 10.1016/S0006-3495(96)79574-7 10.1083/jcb.17.1.208 10.1038/ng.487 10.1016/S0896-6273(00)80886-7 10.1002/mds.21007 10.1074/jbc.M609821200 10.1523/JNEUROSCI.4977-09.2010 10.1523/JNEUROSCI.20-09-03214.2000 10.1074/jbc.M700368200 10.1038/nature02261 10.1016/S0002-9440(10)64553-1 10.1074/jbc.M507624200 10.1002/emmm.200900006 10.1523/JNEUROSCI.22-20-08797.2002 10.1074/jbc.M208194200 10.1074/jbc.M808515200 10.1002/j.1460-2075.1991.tb04966.x 10.1073/pnas.96.22.12571 10.1007/s00401-006-0114-4 10.1021/bi002030k 10.1016/j.cell.2005.09.028 10.1016/j.jmb.2009.05.066 10.1038/42166 10.1523/JNEUROSCI.3809-03.2004 10.1074/jbc.M501599200 10.1529/biophysj.105.062539 10.1038/ncb2012 10.1038/33416 10.1073/pnas.0407307101 10.2174/138920306779025675 10.1111/j.1600-0854.2008.00853.x 10.1074/jbc.273.41.26292 10.1523/JNEUROSCI.4308-05.2006 10.1038/nature04779 10.1001/jama.296.6.661 10.1038/nrn2233 10.1016/S1097-2765(00)80391-3 10.1073/pnas.0710685105 10.1016/j.jmb.2009.10.066 10.1126/science.1129462 10.1074/jbc.M512292200 10.1371/journal.pone.0005701 10.1523/JNEUROSCI.4564-06.2007 10.1016/S0006-3495(03)74590-1 10.1007/s12013-007-0014-9 10.1074/jbc.M411805200 10.1523/JNEUROSCI.20-17-06365.2000 10.1016/j.cell.2006.10.030 10.1002/cbic.200800238 10.1093/hmg/ddi396 10.1139/g06-011 10.1073/pnas.0402959101 10.1074/jbc.M305266200 10.1016/S0002-9440(10)63072-6 10.1038/ng.300 10.1021/bi900114z 10.1074/jbc.M709634200 10.1097/01.mol.0000169348.61191.ac 10.1038/nrm2275 10.1073/pnas.0501282102 10.1074/jbc.M808895200 10.1038/ng.485 10.1074/jbc.M109.035774 10.1074/jbc.M710012200 10.1016/S0304-3940(03)00941-8 10.1016/j.yexcr.2008.03.012 10.1139/G08-085 10.1007/BF00232676 10.1021/bi00567a011 10.1074/jbc.R800011200 10.1074/jbc.M806902200 10.1016/S0140-6736(04)17104-3 10.1523/JNEUROSCI.3821-06.2006 10.1038/nature04788 10.1111/j.1432-1033.2004.04250.x 10.1074/jbc.273.16.9443 10.1016/j.neulet.2008.05.005 10.1073/pnas.0807826105 10.1146/annurev.biochem.72.121801.161504 10.1016/S0896-6273(03)00024-2 10.1007/s00249-006-0097-z 10.1021/bi052344d 10.1523/JNEUROSCI.0719-07.2007 10.1074/jbc.M606059200 10.1093/nar/gkn084 10.1016/0005-2736(94)90156-2 10.1074/jbc.M401076200 10.1038/nature01135 10.1021/bi00558a005 10.1126/science.1096284 10.1529/biophysj.106.090043 10.1523/JNEUROSCI.5537-06.2007 10.1529/biophysj.105.071415 10.1523/JNEUROSCI.08-08-02804.1988 10.1074/jbc.M306769200 10.1007/s00018-008-7589-1 10.1038/nrm2101 10.1073/pnas.0809232106 10.1074/jbc.M401135200 10.1111/j.1471-4159.2007.04764.x 10.1523/JNEUROSCI.2559-04.2004 10.1016/j.bbamem.2008.01.012 10.1016/0005-2736(82)90038-4 10.1007/978-1-59745-365-3_30 10.1007/s002329900535 10.1038/emboj.2009.257 10.1371/journal.pone.0002455 10.1021/ja801594s 10.1016/j.biocel.2009.05.008 10.1523/JNEUROSCI.3088-08.2008 10.1016/S0959-440X(03)00107-6 10.1126/science.1090278 10.1021/bi00517a023 10.1016/j.cub.2004.02.004 10.1074/jbc.M309204200 10.1016/S0006-291X(03)00050-0 10.1111/j.1460-9568.2006.05210.x 10.1073/pnas.0406283101 |
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| References | Chen M, Margittai M, Chen J, Langen R (2007) Investigation of alpha-synuclein fibril structure by site-directed spin labeling. J Biol Chem 282: 24970-24979 Nuscher B, Kamp F, Mehnert T, Odoy S, Haass C, Kahle PJ, Beyer K (2004) α-synuclein has a high affinity for packing defects in a bilayer membrane. A thermodynamics study. J Biol Chem 21: 21966-21975 Dennison SM, Bowen ME, Brunger AT, Lentz BR (2006) Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion. Biophys J 90: 1661-1675 Kostka M, Hogen T, Danzer KM, Levin J, Habeck M, Wirth A, Wagner R, Glabe CG, Finger S, Heinzelmann U, Garidel P, Duan W, Ross CA, Kretzschmar H, Giese A (2008) Single-particle characterization of iron-induced pore-forming alpha -synuclein oligomers. J Biol Chem 283: 10992-11003 Ramakrishnan M, Jensen PH, Marsh D (2006) Association of alpha-synuclein and mutants with lipid membranes: spin-label ESR and polarized IR. Biochemistry 45: 3386-3395 Shavali S, Brown-Borg HM, Ebadi M, Porter J (2008) Mitochondrial localization of alpha-synuclein protein in alpha-synuclein overexpressing cells. Neurosci Lett 439: 125-128 Ulmer TS, Bax A, Cole NB, Nussbaum RL (2005) Structure and dynamics of micelle-bound human alpha-synuclein. J Biol Chem 280: 9595-9603 Harder Z, Zunino R, McBride H (2004) Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol 14: 340-345 Ishihara N, Jofuku A, Eura Y, Mihara K (2003) Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells. Biochem Biophys Res Commun 301: 891-898 Grundemann J, Schlaudraff F, Haeckel O, Liss B (2008) Elevated alpha-synuclein mRNA levels in individual UV-laser-microdissected dopaminergic substantia nigra neurons in idiopathic Parkinson's disease. Nucleic Acids Res 36: e38 Gaber BP, Sheridan JP (1982) Kinetic and thermodynamic studies of the fusion of small unilamellar phospholipid vesicles. Biochim Biophys Acta 685: 87-93 Jo E, Darabie AA, Han K, Tandon A, Fraser PE, McLaurin J (2004) alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis. Eur J Biochem 271: 3180-3189 Beyer K (2007) Mechanistic aspects of Parkinson's disease. α-synuclein and the biomembrane. Cell Biochem Biophys 47: 285-299 Haywood AF, Staveley BE (2006) Mutant alpha-synuclein-induced degeneration is reduced by parkin in a fly model of Parkinson's disease. Genome 49: 505-510 Detmer SA, Chan DC (2007) Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 8: 870-879 Sandebring A, Thomas KJ, Beilina A, van der Brug M, Cleland MM, Ahmad R, Miller DW, Zambrano I, Cowburn RF, Behbahani H, Cedazo-Minguez A, Cookson MR (2009) Mitochondrial alterations in PINK1 deficient cells are influenced by calcineurin-dependent dephosphorylation of dynamin-related protein 1. PLoS One 4: e5701 Giannakis E, Pacifico J, Smith DP, Hung LW, Masters CL, Cappai R, Wade JD, Barnham KJ (2008) Dimeric structures of alpha-synuclein bind preferentially to lipid membranes. Biochim Biophys Acta 1778: 1112-1119 Pantazatos DP, MacDonald RC (1999) Directly observed membrane fusion between oppositely charged phospholipid bilayers. J Membr Biol 170: 27-38 Tamm LK, Crane J, Kiessling V (2003) Membrane fusion: a structural perspective on the interplay of lipids and proteins. Curr Opin Struct Biol 13: 453-466 Clark IE, Dodson MW, Jiang C, Cao JH, Huh JR, Seol JH, Yoo SJ, Hay BA, Guo M (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441: 1162-1166 Labrousse AM, Zappaterra MD, Rube DA, VanderBliek AM (1999) C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane. Mol Cell 4: 815-826 Chandra S, Gallardo G, Fernandez-Chacon R, Schluter OM, Sudhof TC (2005) Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell 123: 383-396 Wilschut J, Düzgünes N, Fraley R, Papahadjopoulos D (1980) Studies on the mechanism of membrane fusion: kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicles contents. Biochemistry 1980: 6011-6021 Chandra S, Fornai F, Kwon HB, Yazdani U, Atasoy D, Liu X, Hammer RE, Battaglia G, German DC, Castillo PE, Sudhof TC (2004) Double-knockout mice for alpha- and beta-synucleins: effect on synaptic functions. Proc Natl Acad Sci USA 101: 14966-14971 Uversky VN (2007) Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation. J Neurochem 103: 17-37 Derksen A, Gantz D, Small DM (1996) Calorimetry of apolipoprotein-A1 binding to phosphatidylcholine-triolein-cholesterol emulsions. Biophys J 70: 330-338 Iwai A, Masliah E, Yoshimoto M, Ge N, Flanagan L, de Silva HA, Kittel A, Saitoh T (1995) The precursor protein of non-A beta component of Alzheimer′s disease amyloid is a presynaptic protein of the central nervous system. Neuron 14: 467-475 Reynolds ES (1963) The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol 17: 208-212 van Ham TJ, Esposito A, Kumita JR, Hsu ST, Kaminski Schierle GS, Kaminski CF, Dobson CM, Nollen EA, Bertoncini CW (2010) Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation. J Mol Biol 395: 627-642 Hasegawa T, Matsuzaki M, Takeda A, Kikuchi A, Akita H, Perry G, Smith MA, Itoyama Y (2004) Accelerated alpha-synuclein aggregation after differentiation of SH-SY5Y neuroblastoma cells. Brain Res 1013: 51-59 Tsika E, Moysidou M, Guo J, Cushman M, Gannon P, Sandaltzopoulos R, Giasson BI, Krainc D, Ischiropoulos H, Mazzulli JR (2010) Distinct region-specific alpha-synuclein oligomers in A53T transgenic mice: implications for neurodegeneration. J Neurosci 30: 3409-3418 Canet-Aviles RM, Wilson MA, Miller DW, Ahmad R, McLendon C, Bandyopadhyay S, Baptista MJ, Ringe D, Petsko GA, Cookson MR (2004) The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc Natl Acad Sci USA 101: 9103-9108 Henn IH, Bouman L, Schlehe JS, Schlierf A, Schramm JE, Wegener E, Nakaso K, Culmsee C, Berninger B, Krappmann D, Tatzelt J, Winklhofer KF (2007) Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J Neurosci 27: 1868-1878 Fujita Y, Ohama E, Takatama M, Al-Sarraj S, Okamoto K (2006) Fragmentation of Golgi apparatus of nigral neurons with alpha-synuclein-positive inclusions in patients with Parkinson's disease. Acta Neuropathol 112: 261-265 Schullery SE, Schmidt CF, Felgner P, Tillack TW, Thompson TE (1980a) Fusion of dipalmitoylphosphatidylcholine vesicles. Biochemistry 19: 3919-3923 Lentz BR (2007) PEG as a tool to gain insight into membrane fusion. Eur Biophys J 36: 315-326 Gitler AD, Chesi A, Geddie ML, Strathearn KE, Hamamichi S, Hill KJ, Caldwell KA, Caldwell GA, Cooper AA, Rochet JC, Lindquist S (2009) Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet 41: 308-315 Davidson WS, Jonas A, Clayton DF, George JM (1998) Stabilization of α-synuclein secondary structue upon bindung to synthetic membranes. J Biol Chem 273: 9443-9449 Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, Minoshima S, Yokochi M, Mizuno Y, Shimizu N (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-608 Haque ME, McIntosh TJ, Lentz BR (2001) Influence of lipid composition on physical properties and PEG-mediated fusion of curved and uncurved model membrane vesicles: 'nature's own fusogenic lipid bilayer'. Biochemistry 40: 4340-4348 Kim RH, Smith PD, Aleyasin H, Hayley S, Mount MP, Pownall S, Wakeham A, You-Ten AJ, Kalia SK, Horne P, Westaway D, Lozano AM, Anisman H, Park DS, Mak TW (2005) Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc Natl Acad Sci USA 102: 5215-5220 Orth M, Tabrizi SJ, Schapira AH, Cooper JM (2003) Alpha-synuclein expression in HEK293 cells enhances the mitochondrial sensitivity to rotenone. Neurosci Lett 351: 29-32 Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998) SNAREpins: minimal machinery for membrane fusion. Cell 92: 759-772 Yavich L, Tanila H, Vepsalainen S, Jakala P (2004) Role of alpha-synuclein in presynaptic dopamine recruitment. J Neurosci 24: 11165-11170 Duvezin-Caubet S, Jagasia R, Wagener J, Hofmann S, Trifunovic A, Hansson A, Chomyn A, Bauer MF, Attardi G, Larsson NG, Neupert W, Reichert AS (2006) Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology. J Biol Chem 281: 37972-37979 Larsen KE, Schmitz Y, Troyer MD, Mosharov E, Dietrich P, Quazi AZ, Savalle M, Nemani V, Chaudhry FA, Edwards RH, Stefanis L, Sulzer D (2006) α-Synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis. J Neurosci 26: 11915-11922 Devi L, Raghavendran V, Prabhu BM, Avadhani NG, Anandatheerthavarada HK (2008) Mitochondrial import and accumulation of {alpha}-sy. J Biol Chem 283: 9089-9100 Herndon LA, Schmeissner PJ, Dudaronek JM, Brown PA, Listner KM, Sakano Y, Paupard MC, Hall DH, Driscoll M (2002) Stochastic and genetic factors influence tissue-specific decline in ageing C. elegans. Nature 419: 808-814 Jensen PH, Nielsen MS, Jakes R, Dotti CG, Goedert M (1998) Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J Biol Chem 273: 26292-26294 Neuspiel M, Zunino R, Gangaraju S, Rippstein P, McBride H (2005) Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization. J Biol Chem 280: 25060-25070 Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, Lee MJ, Chaudhry FA, Nicoli RA, Edwards RH ( Lee, Langen, Hummel, Gray, Winkler (CR73) 2004; 101 Ishihara, Jofuku, Eura, Mihara (CR55) 2003; 301 Geisler, Holmstrom, Skujat, Fiesel, Rothfuss, Kahle, Springer (CR35) 2010; 12 Maroteaux, Campanelli, Scheller (CR81) 1988; 8 Kayed, Pensalfini, Margol, Sokolov, Sarsoza, Head, Hall, Glabe (CR64) 2009; 284 Hsu, Sagara, Arroyo, Rockenstein, Sisk, Mallory, Wong, Takenouchi, Hashimoto, Masliah (CR53) 2000; 157 Palacino, Sagi, Goldberg, Krauss, Motz, Wacker, Klose, Shen (CR94) 2004; 279 Chernomordik, Kozlov (CR12) 2003; 72 Niemann, Ruegg, La Padula, Schenone, Suter (CR90) 2005; 170 Malka, Aure, Goffart, Spelbrink, Rojo (CR79) 2007; 372 Drescher, Godschalk, Veldhuis, van Rooijen, Subramaniam, Huber (CR28) 2008; 9 Chen, Margittai, Chen, Langen (CR9) 2007; 282 Ramakrishnan, Jensen, Marsh (CR101) 2006; 45 Rostaing, Weimer, Jorgensen, Triller, Bessereau (CR103) 2004; 52 Uversky (CR122) 2002; 269 Chandra, Gallardo, Fernandez‐Chacon, Schluter, Sudhof (CR8) 2005; 123 Spillantini, Schmidt, Lee, Trojanowski, Jakes, Goedert (CR113) 1997; 388 Sandebring, Thomas, Beilina, van der Brug, Cleland, Ahmad, Miller, Zambrano, Cowburn, Behbahani, Cedazo‐Minguez, Cookson (CR104) 2009; 4 Kitada, Asakawa, Hattori, Matsumine, Yamamura, Minoshima, Yokochi, Mizuno, Shimizu (CR66) 1998; 392 Weber, Zemelman, McNew, Westermann, Gmachl, Parlati, Sollner, Rothman (CR127) 1998; 92 Nuscher, Kamp, Mehnert, Odoy, Haass, Kahle, Beyer (CR91) 2004; 21 Ulmer, Bax, Cole, Nussbaum (CR121) 2005; 280 Henn, Gostner, Lackner, Tatzelt, Winklhofer (CR50) 2005; 92 Chandra, Fornai, Kwon, Yazdani, Atasoy, Liu, Hammer, Battaglia, German, Castillo, Sudhof (CR7) 2004; 101 Kamp, Beyer (CR62) 2006; 281 Chiba‐Falek, Lopez, Nussbaum (CR13) 2006; 21 Neuspiel, Zunino, Gangaraju, Rippstein, McBride (CR88) 2005; 280 Weinreb, Lentz (CR128) 2007; 92 Haywood, Staveley (CR48) 2006; 49 Henn, Bouman, Schlehe, Schlierf, Schramm, Wegener, Nakaso, Culmsee, Berninger, Krappmann, Tatzelt, Winklhofer (CR49) 2007; 27 Kramer, Schulz‐Schaeffer (CR68) 2007; 27 Shavali, Brown‐Borg, Ebadi, Porter (CR109) 2008; 439 Okita, Sato, Schroeder (CR92) 2004; 36 Bodner, Dobson, Bax (CR4) 2009; 390 Chen, Arac, Wang, Gilpin, Zimmerberg, Rizo (CR10) 2006; 90 Westermann (CR129) 2008; 283 Gaber, Sheridan (CR34) 1982; 685 Tamm, Crane, Kiessling (CR116) 2003; 13 Lentz (CR75) 2007; 36 Satake, Nakabayashi, Mizuta, Hirota, Ito, Kubo, Kawaguchi, Tsunoda, Watanabe, Takeda, Tomiyama, Nakashima, Hasegawa, Obata, Yoshikawa, Kawakami, Sakoda, Yamamoto, Hattori, Murata (CR105) 2009; 41 Cole, Dieuliis, Leo, Mitchell, Nussbaum (CR16) 2008; 314 Jao, Hegde, Chen, Haworth, Langen (CR57) 2008; 105 Gosavi, Lee, Lee, Patel, Lee (CR41) 2002; 277 Pantazatos, MacDonald (CR95) 1999; 170 Beyer (CR3) 2007; 47 Cornell, Taneva (CR18) 2006; 7 Ferreon, Gambin, Lemke, Deniz (CR32) 2009; 106 CR52 Dagda, Cherra, Kulich, Tandon, Park, Chu (CR19) 2009; 284 Larsen, Schmitz, Troyer, Mosharov, Dietrich, Quazi, Savalle, Nemani, Chaudhry, Edwards, Stefanis, Sulzer (CR70) 2006; 26 Karpinar, Balija, Kugler, Opazo, Rezaei‐Ghaleh, Wender, Kim, Taschenberger, Falkenburger, Heise, Kumar, Riedel, Fichtner, Voigt, Braus, Giller, Becker, Herzig, Baldus, Jackle (CR63) 2009; 28 Murphy, Rueter, Trojanowski, Lee (CR85) 2000; 20 Dennison, Bowen, Brunger, Lentz (CR22) 2006; 90 Gorner, Holtorf, Waak, Pham, Vogt‐Weisenhorn, Wurst, Haass, Kahle (CR40) 2007; 282 Davidson, Jonas, Clayton, George (CR21) 1998; 273 Morais, Verstreken, Roethig, Smet, Snellinx, Vanbrabant, Haddad, Frezza, Mandemakers, Vogt‐Weisenhorn, Van Coster, Wurst, Scorrano, De Strooper (CR84) 2009; 1 Ibanez, Bonnet, Debarges, Lohmann, Tison, Pollak, Agid, Durr, Brice (CR54) 2004; 364 Lutz, Exner, Fett, Schlehe, Kloos, Laemmermann, Brunner, Kurz‐Drexler, Vogel, Reichert, Bouman, Vogt‐Weisenhorn, Wurst, Tatzelt, Haass, Winklhofer (CR78) 2009; 284 Park, Lee, Lee, Kim, Song, Kim, Bae, Kim, Shong, Kim, Chung (CR98) 2006; 441 Martin, Pan, Price, Sterling, Copeland, Jenkins, Price, Lee (CR82) 2006; 26 Abeliovich, Schmitz, Farinas, Choi‐Lundberg, Ho, Castillo, Shinsky, Verdugo, Armanini, Ryan, Hynes, Phillips, Sulzer, Rosenthal (CR1) 2000; 25 Wood‐Kaczmar, Gandhi, Yao, Abramov, Miljan, Keen, Stanyer, Hargreaves, Klupsch, Deas, Downward, Mansfield, Jat, Taylor, Heales, Duchen, Latchman, Tabrizi, Wood (CR132) 2008; 3 Lee, Khoshaghideh, Patel, Lee (CR72) 2004; 24 Piomelli, Astarita, Rapaka (CR100) 2007; 8 Mello, Kramer, Stinchcomb, Ambros (CR83) 1991; 10 Kim, Smith, Aleyasin, Hayley, Mount, Pownall, Wakeham, You‐Ten, Kalia, Horne, Westaway, Lozano, Anisman, Park, Mak (CR65) 2005; 102 Zhang, Rowe (CR134) 1994; 1193 Labrousse, Zappaterra, Rube, VanderBliek (CR69) 1999; 4 Duvezin‐Caubet, Jagasia, Wagener, Hofmann, Trifunovic, Hansson, Chomyn, Bauer, Attardi, Larsson, Neupert, Reichert (CR30) 2006; 281 Schullery, Schmidt, Felgner, Tillack, Thompson (CR106) 1980; 19 Detmer, Chan (CR25) 2007; 8 Hasegawa, Matsuzaki, Takeda, Kikuchi, Akita, Perry, Smith, Itoyama (CR47) 2004; 1013 Todd, Staveley (CR117) 2008; 51 Cooper, Gitler, Cashikar, Haynes, Hill, Bhullar, Liu, Xu, Strathearn, Liu, Cao, Caldwell, Caldwell, Marsischky, Kolodner, Labaer, Rochet, Bonini, Lindquist (CR17) 2006; 313 Simon‐Sanchez, Schulte, Bras, Sharma, Gibbs, Berg, Paisan‐Ruiz, Lichtner, Scholz, Hernandez, Kruger, Federoff, Klein, Goate, Perlmutter, Bonin, Nalls, Illig, Gieger, Houlden (CR110) 2009; 41 Takamori, Holt, Stenius, Lemke, Gronborg, Riedel, Urlaub, Schenck, Brugger, Ringler, Muller, Rammner, Grater, Hub, De Groot, Mieskes, Moriyama, Klingauf, Grubmuller, Heuser (CR115) 2006; 127 Smith, Jiang, Pei, Tanaka, Morita, Sawa, Dawson, Dawson, Ross (CR112) 2005; 14 Reynolds (CR102) 1963; 17 Dobson (CR27) 2003; 426 Lee, Khoshaghideh, Lee, Lee (CR71) 2006; 24 Der‐Sarkissian, Jao, Chen, Langen (CR23) 2003; 278 Sharon, Bar‐Joseph, Frosch, Walsh, Hamilton, Selkoe (CR108) 2003; 37 Singleton, Farrer, Johnson, Singleton, Hague, Kachergus, Hulihan, Peuralinna, Dutra, Nussbaum, Lincoln, Crawley, Hanson, Maraganore, Adler, Cookson, Muenter, Baptista, Miller, Blancato (CR111) 2003; 302 Giannakis, Pacifico, Smith, Hung, Masters, Cappai, Wade, Barnham (CR36) 2008; 1778 Iwai, Masliah, Yoshimoto, Ge, Flanagan, de Silva, Kittel, Saitoh (CR56) 1995; 14 Trexler, Rhoades (CR118) 2009; 48 Devi, Raghavendran, Prabhu, Avadhani, Anandatheerthavarada (CR26) 2008; 283 Orth, Tabrizi, Schapira, Cooper (CR93) 2003; 351 Perlmutter, Braun, Sachs (CR99) 2009; 284 Cabin, Shimazu, Murphy, Cole, Gottschalk, McIlwain, Orrison, Chen, Ellis, Paylor, Lu, Nussbaum (CR5) 2002; 22 Nakamura, Nemani, Wallender, Kaehlcke, Ott, Edwards (CR86) 2008; 28 Schullery, Schmidt, Felgner, Tillack, Thompson (CR107) 1980; 19 Jensen, Nielsen, Jakes, Dotti, Goedert (CR58) 1998; 273 Liu, Tucker, Bhalla, Chapman, Weisshaar (CR77) 2005; 89 Canet‐Aviles, Wilson, Miller, Ahmad, McLendon, Bandyopadhyay, Baptista, Ringe, Petsko, Cookson (CR6) 2004; 101 Nemani, Lu, Berge, Nakamura, Onoa, Lee, Chaudhry, Nicoli, Edwards (CR87) 2010; 65 Kostka, Hogen, Danzer, Levin, Habeck, Wirth, Wagner, Glabe, Finger, Heinzelmann, Garidel, Duan, Ross, Kretzschmar, Giese (CR67) 2008; 283 Gitler, Bevis, Shorter, Strathearn, Hamamichi, Su, Caldwell, Caldwell, Rochet, McCaffery, Barlowe, Lindquist (CR37) 2008; 105 Derksen, Gantz, Small (CR24) 1996; 70 Lei, MacDonald (CR74) 2003; 85 van Ham, Esposito, Kumita, Hsu, Kaminski Schierle, Kaminski, Dobson, Nollen, Bertoncini (CR125) 2010; 395 Drescher, Veldhuis, van Rooijen, Milikisyants, Subramaniam, Huber (CR29) 2008; 130 Kahle, Neumann, Ozmen, Muller, Jacobsen, Schindzielorz, Okochi, Leimer, van Der Putten, Probst, Kremmer, Kretzschmar, Haass (CR60) 2000; 20 Gursky (CR43) 2005; 16 Wilschut, Düzgünes, Fraley, Papahadjopoulos (CR130) 1980; 1980 Uversky (CR123) 2007; 103 Winklhofer, Henn, Kay‐Jackson, Heller, Tatzelt (CR131) 2003; 278 CR14 Maraganore, de Andrade, Elbaz, Farrer, Ioannidis, Kruger, Rocca, Schneider, Lesnick, Lincoln, Hulihan, Aasly, Ashizawa, Chartier‐Harlin, Checkoway, Ferrarese, Hadjigeorgiou, Hattori, Kawakami, Lambert (CR80) 2006; 296 Struck, Hoekstra, Pagano (CR114) 1981; 20 Davidson, Yellon, Duchen (CR20) 2007; 372 Ulmer, Bax (CR120) 2005; 280 Waak, Weber, Gorner, Schall, Ichijo, Stehle, Kahle (CR126) 2009; 284 Jo, Darabie, Han, Tandon, Fraser, McLaurin (CR59) 2004; 271 Fujita, Ohama, Takatama, Al‐Sarraj, Okamoto (CR33) 2006; 112 Parihar, Parihar, Fujita, Hashimoto, Ghafourifar (CR97) 2009; 41 Tsika, Moysidou, Guo, Cushman, Gannon, Sandaltzopoulos, Giasson, Krainc, Ischiropoulos, Mazzulli (CR119) 2010; 30 Gorner, Holtorf, Odoy, Nuscher, Yamamoto, Regula, Beyer, Haass, Kahle (CR39) 2004; 279 Exner, Treske, Paquet, Holmstrom, Schiesling, Gispert, Carballo‐Carbajal, Berg, Hoepken, Gasser, Kruger, Winklhofer, Vogel, Reichert, Auburger, Kahle, Schmid, Haass (CR31) 2007; 27 Gitler, Chesi, Geddie, Strathearn, Hamamichi, Hill, Caldwell, Caldwell, Cooper, Rochet, Lindquist (CR38) 2009; 41 Haass, Selkoe (CR44) 2007; 8 Nickel, Weber, McNew, Parlati, Sollner, Rothman (CR89) 1999; 96 Li, Yang, Guo, Ren, Zha, Cheng, Cai (CR76) 2007; 18 Ben Gedalya, Loeb, Israeli, Altschuler, Selkoe, Sharon (CR2) 2009; 10 Parihar, Parihar, Fujita, Hashimoto, Ghafourifar (CR96) 2008; 65 Yavich, Tanila, Vepsalainen, Jakala (CR133) 2004; 24 Haque, McIntosh, Lentz (CR45) 2001; 40 Herndon, Schmeissner, Dudaronek, Brown, Listner, Sakano, Paupard, Hall, Driscoll (CR51) 2002; 419 Chernomordik, Kozlov, Zimmerberg (CR11) 1995; 146 Clark, Dodson, Jiang, Cao, Huh, Seol, Yoo, Hay, Guo (CR15) 2006; 441 Kahle, Neumann, Ozmen, Müller, Odoy, Okamoto, Jacobsen, Iwatsubo, Trojanowski, Takahashi, Wakabayashi, Bogdanovic, Riederer, Kreschmar, Haass (CR61) 2001; 159 Valente, Abou‐Sleiman, Caputo, Muqit, Harvey, Gispert, Ali, Del Turco, Bentivoglio, Healy, Albanese, Nussbaum, Gonzalez‐Maldonado, Deller, Salvi, Cortelli, Gilks, Latchman, Harvey, Dallapiccola (CR124) 2004; 304 Harder, Zunino, McBride (CR46) 2004; 14 Grundemann, Schlaudraff, Haeckel, Liss (CR42) 2008; 36 2010; 12 2004; 21 2007; 103 2005; 170 2008a; 9 1991; 10 2002; 277 1999; 170 2004; 24 2008; 36 2006; 296 2008; 105 1996; 70 2003; 278 1980a; 19 2001; 40 1998; 392 1998; 273 2004b; 101 1997; 388 2009; 10 2006; 24 2006; 21 2005; 102 2004; 36 2006; 26 2008; 28 2007; 8 2002; 269 1998; 92 2006; 281 2004; 1013 2010; 30 2006; 441 2007; 18 1980; 1980 2008b; 130 2007; 282 2004a; 24 2003; 37 2007; 92 2002; 419 1982; 685 2008; 51 2004; 304 2006; 112 2005; 89 1981; 20 2004; 52 2004; 279 2006; 45 2005; 123 2006; 49 1980b; 19 2004; 271 1995; 146 2005; 92 2005; 16 2001; 159 2009; 106 2005; 14 2004; 364 2009; 41 2003; 13 2008; 3 2007; 36 2009; 48 2003; 351 2010; 65 2007; 372 2008; 439 2010; 395 2008; 314 2008; 65 1999; 96 2009; 284 2006; 127 1994; 1193 2003; 85 2007; 27 2004; 101 2006; 90 2000; 25 2000; 157 2010 1995; 14 2000; 20 2006; 7 1999; 4 2003 2008; 1778 2003; 72 2006; 313 2008; 283 2009; 28 2005; 280 2003; 426 2009; 390 2004; 14 1988; 8 2002; 22 2009; 4 2003; 302 2003; 301 2009; 1 1963; 17 2007; 47 Cooper AA (emboj2010223-b17) 2006; 313 Geisler S (emboj2010223-b35) 2010; 12 Cole NB (emboj2010223-b16) 2008; 314 Giannakis E (emboj2010223-b36) 2008; 1778 Ben Gedalya T (emboj2010223-b2) 2009; 10 Chandra S (emboj2010223-b7) 2004; 101 Niemann A (emboj2010223-b90) 2005; 170 Lei G (emboj2010223-b74) 2003; 85 Devi L (emboj2010223-b26) 2008; 283 Lee HJ (emboj2010223-b71) 2006; 24 Duvezin-Caubet S (emboj2010223-b30) 2006; 281 Nickel W (emboj2010223-b89) 1999; 96 Chernomordik L (emboj2010223-b11) 1995; 146 Larsen KE (emboj2010223-b70) 2006; 26 Dobson CM (emboj2010223-b27) 2003; 426 Clark IE (emboj2010223-b15) 2006; 441 Herndon LA (emboj2010223-b51) 2002; 419 Winklhofer KF (emboj2010223-b131) 2003; 278 Reynolds ES (emboj2010223-b102) 1963; 17 Haass C (emboj2010223-b44) 2007; 8 Gorner K (emboj2010223-b40) 2007; 282 Labrousse AM (emboj2010223-b69) 1999; 4 Yavich L (emboj2010223-b133) 2004; 24 Jao CC (emboj2010223-b57) 2008; 105 Drescher M (emboj2010223-b28) 2008a; 9 Neuspiel M (emboj2010223-b88) 2005; 280 Simon-Sanchez J (emboj2010223-b110) 2009; 41 Wood-Kaczmar A (emboj2010223-b132) 2008; 3 Okita C (emboj2010223-b92) 2004; 36 Der-Sarkissian A (emboj2010223-b23) 2003; 278 Lutz AK (emboj2010223-b78) 2009; 284 Ramakrishnan M (emboj2010223-b101) 2006; 45 Perlmutter JD (emboj2010223-b99) 2009; 284 Todd AM (emboj2010223-b117) 2008; 51 Pantazatos DP (emboj2010223-b95) 1999; 170 emboj2010223-b14 Martin LJ (emboj2010223-b82) 2006; 26 Westermann B (emboj2010223-b129) 2008; 283 Parihar MS (emboj2010223-b96) 2008; 65 Weinreb G (emboj2010223-b128) 2007; 92 Maroteaux L (emboj2010223-b81) 1988; 8 Kim RH (emboj2010223-b65) 2005; 102 Singleton AB (emboj2010223-b111) 2003; 302 Derksen A (emboj2010223-b24) 1996; 70 Chandra S (emboj2010223-b8) 2005; 123 Fujita Y (emboj2010223-b33) 2006; 112 Bodner CR (emboj2010223-b4) 2009; 390 Nemani VM (emboj2010223-b87) 2010; 65 Lee HJ (emboj2010223-b72) 2004a; 24 Drescher M (emboj2010223-b29) 2008b; 130 Parihar MS (emboj2010223-b97) 2009; 41 Trexler A (emboj2010223-b118) 2009; 48 Rostaing P (emboj2010223-b103) 2004; 52 Piomelli D (emboj2010223-b100) 2007; 8 Satake W (emboj2010223-b105) 2009; 41 Sandebring A (emboj2010223-b104) 2009; 4 Chen X (emboj2010223-b10) 2006; 90 Mello CC (emboj2010223-b83) 1991; 10 Palacino JJ (emboj2010223-b94) 2004; 279 Jensen PH (emboj2010223-b58) 1998; 273 Gosavi N (emboj2010223-b41) 2002; 277 Abeliovich A (emboj2010223-b1) 2000; 25 Weber T (emboj2010223-b127) 1998; 92 Schullery SE (emboj2010223-b106) 1980a; 19 Sharon R (emboj2010223-b108) 2003; 37 Spillantini MG (emboj2010223-b113) 1997; 388 Ibanez P (emboj2010223-b54) 2004; 364 Ferreon AC (emboj2010223-b32) 2009; 106 Uversky VN (emboj2010223-b122) 2002; 269 Shavali S (emboj2010223-b109) 2008; 439 Kayed R (emboj2010223-b64) 2009; 284 Wilschut J (emboj2010223-b130) 1980; 1980 Orth M (emboj2010223-b93) 2003; 351 Malka F (emboj2010223-b79) 2007; 372 Gorner K (emboj2010223-b39) 2004; 279 Henn IH (emboj2010223-b50) 2005; 92 Maraganore DM (emboj2010223-b80) 2006; 296 Haque ME (emboj2010223-b45) 2001; 40 Detmer SA (emboj2010223-b25) 2007; 8 Chiba-Falek O (emboj2010223-b13) 2006; 21 Kamp F (emboj2010223-b62) 2006; 281 Morais VA (emboj2010223-b84) 2009; 1 Gaber BP (emboj2010223-b34) 1982; 685 Schullery SE (emboj2010223-b107) 1980b; 19 Dagda RK (emboj2010223-b19) 2009; 284 Ulmer TS (emboj2010223-b121) 2005; 280 Waak J (emboj2010223-b126) 2009; 284 Gitler AD (emboj2010223-b38) 2009; 41 Canet-Aviles RM (emboj2010223-b6) 2004; 101 Harder Z (emboj2010223-b46) 2004; 14 Kramer ML (emboj2010223-b68) 2007; 27 Karpinar DP (emboj2010223-b63) 2009; 28 Chen M (emboj2010223-b9) 2007; 282 Kahle PJ (emboj2010223-b60) 2000; 20 Hasegawa T (emboj2010223-b47) 2004; 1013 Li WW (emboj2010223-b76) 2007; 18 Hsu LJ (emboj2010223-b53) 2000; 157 Ulmer TS (emboj2010223-b120) 2005; 280 Ishihara N (emboj2010223-b55) 2003; 301 Tamm LK (emboj2010223-b116) 2003; 13 Struck DK (emboj2010223-b114) 1981; 20 Liu T (emboj2010223-b77) 2005; 89 Takamori S (emboj2010223-b115) 2006; 127 Henn IH (emboj2010223-b49) 2007; 27 Beyer K (emboj2010223-b3) 2007; 47 Nuscher B (emboj2010223-b91) 2004; 21 Murphy DD (emboj2010223-b85) 2000; 20 Tsika E (emboj2010223-b119) 2010; 30 Uversky VN (emboj2010223-b123) 2007; 103 Grundemann J (emboj2010223-b42) 2008; 36 Park J (emboj2010223-b98) 2006; 441 Jo E (emboj2010223-b59) 2004; 271 emboj2010223-b52 Cabin DE (emboj2010223-b5) 2002; 22 Smith WW (emboj2010223-b112) 2005; 14 Nakamura K (emboj2010223-b86) 2008; 28 Davidson WS (emboj2010223-b21) 1998; 273 Iwai A (emboj2010223-b56) 1995; 14 Valente EM (emboj2010223-b124) 2004; 304 Gursky O (emboj2010223-b43) 2005; 16 Lentz BR (emboj2010223-b75) 2007; 36 Davidson SM (emboj2010223-b20) 2007; 372 Dennison SM (emboj2010223-b22) 2006; 90 Cornell RB (emboj2010223-b18) 2006; 7 Exner N (emboj2010223-b31) 2007; 27 Zhang F (emboj2010223-b134) 1994; 1193 Lee JC (emboj2010223-b73) 2004b; 101 Kitada T (emboj2010223-b66) 1998; 392 Kahle PJ (emboj2010223-b61) 2001; 159 Chernomordik LV (emboj2010223-b12) 2003; 72 Gitler AD (emboj2010223-b37) 2008; 105 Kostka M (emboj2010223-b67) 2008; 283 Haywood AF (emboj2010223-b48) 2006; 49 van Ham TJ (emboj2010223-b125) 2010; 395 16519533 - Biochemistry. 2006 Mar 14;45(10):3386-95 19915575 - Nat Genet. 2009 Dec;41(12):1308-12 13986422 - J Cell Biol. 1963 Apr;17:208-12 20577776 - Cell Mol Life Sci. 2010 Oct;67(20):3435-47 14527322 - Annu Rev Biochem. 2003;72:175-207 17287515 - J Neurosci. 2007 Feb 7;27(6):1405-10 12388586 - J Neurosci. 2002 Oct 15;22(20):8797-807 19745811 - EMBO J. 2009 Oct 21;28(20):3256-68 9560156 - Nature. 1998 Apr 9;392(6676):605-8 15181200 - Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):9103-8 8054342 - Biochim Biophys Acta. 1994 Aug 3;1193(2):219-25 17882252 - Nat Rev Neurosci. 2007 Oct;8(10):743-54 18162536 - Proc Natl Acad Sci U S A. 2008 Jan 8;105(1):145-50 14985362 - J Biol Chem. 2004 Apr 30;279(18):18614-22 15891389 - Curr Opin Lipidol. 2005 Jun;16(3):287-94 10777786 - J Neurosci. 2000 May 1;20(9):3214-20 16269331 - Cell. 2005 Nov 4;123(3):383-96 19492085 - PLoS One. 2009;4(5):e5701 18261456 - Biochim Biophys Acta. 2008 Apr;1778(4):1112-9 15784737 - Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5215-20 18245082 - J Biol Chem. 2008 Apr 4;283(14):9089-100 8770209 - Biophys J. 1996 Jan;70(1):330-8 20152114 - Neuron. 2010 Jan 14;65(1):66-79 19088817 - Genome. 2008 Dec;51(12):1040-6 16767175 - Genome. 2006 May;49(5):505-10 16794039 - Science. 2006 Jul 21;313(5785):324-8 15536128 - Proc Natl Acad Sci U S A. 2004 Nov 23;101(47):16466-71 19182805 - Nat Genet. 2009 Mar;41(3):308-15 18440504 - Exp Cell Res. 2008 Jun 10;314(10):2076-89 15878861 - J Biol Chem. 2005 Jul 1;280(26):25060-70 10398758 - J Membr Biol. 1999 Jul 1;170(1):27-38 20098416 - Nat Cell Biol. 2010 Feb;12(2):119-31 16339880 - Biophys J. 2006 Mar 1;90(5):1661-75 12815044 - J Biol Chem. 2003 Sep 26;278(39):37530-5 7059594 - Biochim Biophys Acta. 1982 Feb 8;685(1):87-93 16455667 - J Biol Chem. 2006 Apr 7;281(14):9251-9 15196967 - Brain Res. 2004 Jul 2;1013(1):51-9 7470445 - Biochemistry. 1980 Dec 23;19(26):6011-21 15615727 - J Biol Chem. 2005 Mar 11;280(10):9595-603 18314743 - Methods Mol Biol. 2007;372:421-30 15590933 - J Neurosci. 2004 Dec 8;24(49):11165-70 17623039 - J Neurochem. 2007 Oct;103(1):17-37 16896109 - JAMA. 2006 Aug 9;296(6):661-70 19460457 - Int J Biochem Cell Biol. 2009 Oct;41(10):2015-24 10535963 - Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12571-6 14550906 - Neurosci Lett. 2003 Nov 6;351(1):29-32 16399671 - J Neurosci. 2006 Jan 4;26(1):41-50 18372247 - J Biol Chem. 2008 May 16;283(20):13501-5 17652776 - Cell Biochem Biophys. 2007;47(2):285-99 10707987 - Neuron. 2000 Jan;25(1):239-52 17168787 - Curr Protein Pept Sci. 2006 Dec;7(6):539-52 15265037 - Eur J Biochem. 2004 Aug;271(15):3180-9 9529252 - Cell. 1998 Mar 20;92(6):759-72 10964942 - J Neurosci. 2000 Sep 1;20(17):6365-73 18821550 - Chembiochem. 2008 Oct 13;9(15):2411-6 17369418 - Biophys J. 2007 Jun 1;92(11):4012-29 7284312 - Biochemistry. 1981 Jul 7;20(14):4093-9 19098006 - J Biol Chem. 2009 Feb 13;284(7):4230-7 17331951 - J Biol Chem. 2007 May 4;282(18):13680-91 19293155 - J Biol Chem. 2009 May 22;284(21):14245-57 15028717 - J Biol Chem. 2004 May 21;279(21):21966-75 9278044 - Nature. 1997 Aug 28;388(6645):839-40 19891973 - J Mol Biol. 2010 Jan 22;395(3):627-42 16166095 - J Biol Chem. 2005 Dec 30;280(52):43179-87 17989306 - J Neurosci. 2007 Nov 7;27(45):12413-8 7563032 - J Membr Biol. 1995 Jul;146(1):1-14 19293380 - Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5645-50 18314714 - Methods Mol Biol. 2007;372:3-16 14688212 - J Histochem Cytochem. 2004 Jan;52(1):1-12 19020024 - J Neurosci. 2008 Nov 19;28(47):12305-17 17245412 - Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12 17314283 - J Neurosci. 2007 Feb 21;27(8):1868-78 18258594 - J Biol Chem. 2008 Apr 18;283(16):10992-1003 16172208 - J Cell Biol. 2005 Sep 26;170(7):1067-78 9545270 - J Biol Chem. 1998 Apr 17;273(16):9443-9 10934145 - Am J Pathol. 2000 Aug;157(2):401-10 17928812 - Nat Rev Mol Cell Biol. 2007 Nov;8(11):870-9 9756856 - J Biol Chem. 1998 Oct 9;273(41):26292-4 20049710 - EMBO Mol Med. 2009 May;1(2):99-111 16361343 - Biophys J. 2006 Mar 15;90(6):2062-74 16672981 - Nature. 2006 Jun 29;441(7097):1162-6 17003040 - J Biol Chem. 2006 Dec 8;281(49):37972-9 16672980 - Nature. 2006 Jun 29;441(7097):1157-61 7857654 - Neuron. 1995 Feb;14(2):467-75 19066219 - Proc Natl Acad Sci U S A. 2008 Dec 16;105(50):19666-71 14593171 - Science. 2003 Oct 31;302(5646):841 12597857 - Neuron. 2003 Feb 20;37(4):583-95 18512917 - J Am Chem Soc. 2008 Jun 25;130(25):7796-7 12351643 - J Biol Chem. 2002 Dec 13;277(50):48984-92 15451225 - Lancet. 2004 Sep 25-Oct 1;364(9440):1169-71 14685248 - Nature. 2003 Dec 18;426(6968):884-90 19915576 - Nat Genet. 2009 Dec;41(12):1303-7 19546216 - J Biol Chem. 2009 Aug 21;284(34):22938-51 17573347 - J Biol Chem. 2007 Aug 24;282(34):24970-9 18560593 - PLoS One. 2008;3(6):e2455 17110340 - Cell. 2006 Nov 17;127(4):831-46 16795004 - Mov Disord. 2006 Oct;21(10):1703-8 12589796 - Biochem Biophys Res Commun. 2003 Feb 21;301(4):891-8 1935914 - EMBO J. 1991 Dec;10(12):3959-70 12972428 - J Biol Chem. 2003 Nov 21;278(47):47199-208 6893276 - Biochemistry. 1980 Aug 19;19(17):3919-23 19126542 - J Biol Chem. 2009 Mar 13;284(11):7177-89 3411354 - J Neurosci. 1988 Aug;8(8):2804-15 11733371 - Am J Pathol. 2001 Dec;159(6):2215-25 19481095 - J Mol Biol. 2009 Jul 24;390(4):775-90 19279012 - J Biol Chem. 2009 May 15;284(20):13843-55 19220042 - Biochemistry. 2009 Mar 24;48(11):2304-6 18514418 - Neurosci Lett. 2008 Jul 11;439(2):125-8 15087508 - Science. 2004 May 21;304(5674):1158-60 17156376 - Eur J Neurosci. 2006 Dec;24(11):3153-62 15465911 - Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14966-71 14972687 - Curr Biol. 2004 Feb 17;14(4):340-5 16855830 - Acta Neuropathol. 2006 Sep;112(3):261-5 12944275 - Biophys J. 2003 Sep;85(3):1585-99 11784292 - Eur J Biochem. 2002 Jan;269(1):2-12 14607841 - J Biol Chem. 2004 Feb 20;279(8):6943-51 20203200 - J Neurosci. 2010 Mar 3;30(9):3409-18 11284690 - Biochemistry. 2001 Apr 10;40(14):4340-8 15038157 - Biotechniques. 2004 Mar;36(3):418-22, 424 17039359 - Eur Biophys J. 2007 Apr;36(4-5):315-26 12397350 - Nature. 2002 Oct 24;419(6909):808-14 17885598 - Neuroreport. 2007 Oct 8;18(15):1543-6 10619028 - Mol Cell. 1999 Nov;4(5):815-26 12948775 - Curr Opin Struct Biol. 2003 Aug;13(4):453-66 18980610 - Traffic. 2009 Feb;10(2):218-34 14985429 - J Neurosci. 2004 Feb 25;24(8):1888-96 18322646 - Cell Mol Life Sci. 2008 Apr;65(7-8):1272-84 16055544 - Biophys J. 2005 Oct;89(4):2458-72 17108165 - J Neurosci. 2006 Nov 15;26(46):11915-22 16239241 - Hum Mol Genet. 2005 Dec 15;14(24):3801-11 15606901 - J Neurochem. 2005 Jan;92(1):114-22 18332041 - Nucleic Acids Res. 2008 Apr;36(7):e38 |
| References_xml | – reference: Perlmutter JD, Braun AR, Sachs JN (2009) Curvature dynamics of α-synuclein familial Parkinson disease mutants: molecular simulations of the micelle- and bilayer-bound forms. J Biol Chem 284: 7177-7189 – reference: Nuscher B, Kamp F, Mehnert T, Odoy S, Haass C, Kahle PJ, Beyer K (2004) α-synuclein has a high affinity for packing defects in a bilayer membrane. A thermodynamics study. J Biol Chem 21: 21966-21975 – reference: Orth M, Tabrizi SJ, Schapira AH, Cooper JM (2003) Alpha-synuclein expression in HEK293 cells enhances the mitochondrial sensitivity to rotenone. Neurosci Lett 351: 29-32 – reference: Chernomordik L, Kozlov MM, Zimmerberg J (1995) Lipids in biological membrane fusion. J Membr Biol 146: 1-14 – reference: Dobson CM (2003) Protein folding and misfolding. Nature 426: 884-890 – reference: Liu T, Tucker WC, Bhalla A, Chapman ER, Weisshaar JC (2005) SNARE-driven, 25-millisecond vesicle fusion in vitro. Biophys J 89: 2458-2472 – reference: Wilschut J, Düzgünes N, Fraley R, Papahadjopoulos D (1980) Studies on the mechanism of membrane fusion: kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicles contents. Biochemistry 1980: 6011-6021 – reference: Duvezin-Caubet S, Jagasia R, Wagener J, Hofmann S, Trifunovic A, Hansson A, Chomyn A, Bauer MF, Attardi G, Larsson NG, Neupert W, Reichert AS (2006) Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology. J Biol Chem 281: 37972-37979 – reference: Der-Sarkissian A, Jao CC, Chen J, Langen R (2003) Structural organization of α-synuclein fibrils studied by site-directed spin labeling. J Biol Chem 278: 37530-37535 – reference: Winklhofer KF, Henn IH, Kay-Jackson PC, Heller U, Tatzelt J (2003) Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones. J Biol Chem 278: 47199-47208 – reference: Murphy DD, Rueter SM, Trojanowski JQ, Lee VM (2000) Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J Neurosci 20: 3214-3220 – reference: Zhang F, Rowe ES (1994) Calorimetric studies of the interactions of cytochrome c with dioleoylphosphatidylglycerol extruded vesicles: ionic strength effects. Biochim Biophys Acta 1193: 219-225 – reference: Sandebring A, Thomas KJ, Beilina A, van der Brug M, Cleland MM, Ahmad R, Miller DW, Zambrano I, Cowburn RF, Behbahani H, Cedazo-Minguez A, Cookson MR (2009) Mitochondrial alterations in PINK1 deficient cells are influenced by calcineurin-dependent dephosphorylation of dynamin-related protein 1. PLoS One 4: e5701 – reference: Piomelli D, Astarita G, Rapaka R (2007) A neuroscientist's guide to lipidomics. Nat Rev 8: 743-754 – reference: Weinreb G, Lentz BR (2007) Analysis of membrane fusion as a two-state sequential process: evaluation of the stalk model. Biophys J 92: 4012-4029 – reference: Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, Bhullar B, Liu K, Xu K, Strathearn KE, Liu F, Cao S, Caldwell KA, Caldwell GA, Marsischky G, Kolodner RD, Labaer J, Rochet JC, Bonini NM, Lindquist S (2006) Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313: 324-328 – reference: Karpinar DP, Balija MB, Kugler S, Opazo F, Rezaei-Ghaleh N, Wender N, Kim HY, Taschenberger G, Falkenburger BH, Heise H, Kumar A, Riedel D, Fichtner L, Voigt A, Braus GH, Giller K, Becker S, Herzig A, Baldus M, Jackle H et al (2009) Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models. EMBO J 28: 3256-3268 – reference: Gorner K, Holtorf E, Waak J, Pham TT, Vogt-Weisenhorn DM, Wurst W, Haass C, Kahle PJ (2007) Structural determinants of the C-terminal helix-kink-helix motif essential for protein stability and survival promoting activity of DJ-1. J Biol Chem 282: 13680-13691 – reference: Gitler AD, Bevis BJ, Shorter J, Strathearn KE, Hamamichi S, Su LJ, Caldwell KA, Caldwell GA, Rochet JC, McCaffery JM, Barlowe C, Lindquist S (2008) The Parkinson's disease protein alpha-synuclein disrupts cellular Rab homeostasis. Proc Natl Acad Sci USA 105: 145-150 – reference: Nakamura K, Nemani VM, Wallender EK, Kaehlcke K, Ott M, Edwards RH (2008) Optical reporters for the conformation of alpha-synuclein reveal a specific interaction with mitochondria. J Neurosci 28: 12305-12317 – reference: Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer′s amyloid beta-peptide. Nat Rev Mol Cell Biol 8: 101-112 – reference: Kostka M, Hogen T, Danzer KM, Levin J, Habeck M, Wirth A, Wagner R, Glabe CG, Finger S, Heinzelmann U, Garidel P, Duan W, Ross CA, Kretzschmar H, Giese A (2008) Single-particle characterization of iron-induced pore-forming alpha -synuclein oligomers. J Biol Chem 283: 10992-11003 – reference: Morais VA, Verstreken P, Roethig A, Smet J, Snellinx A, Vanbrabant M, Haddad D, Frezza C, Mandemakers W, Vogt-Weisenhorn D, Van Coster R, Wurst W, Scorrano L, De Strooper B (2009) Parkinson's disease mutations in PINK1 result in decreased complex I activity and deficient synaptic function. EMBO Mol Med 1: 99-111 – reference: van Ham TJ, Esposito A, Kumita JR, Hsu ST, Kaminski Schierle GS, Kaminski CF, Dobson CM, Nollen EA, Bertoncini CW (2010) Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation. J Mol Biol 395: 627-642 – reference: Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, Gispert S, Ali Z, Del Turco D, Bentivoglio AR, Healy DG, Albanese A, Nussbaum R, Gonzalez-Maldonado R, Deller T, Salvi S, Cortelli P, Gilks WP, Latchman DS, Harvey RJ, Dallapiccola B et al (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304: 1158-1160 – reference: Kramer ML, Schulz-Schaeffer WJ (2007) Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J Neurosci 27: 1405-1410 – reference: Hsu LJ, Sagara Y, Arroyo A, Rockenstein E, Sisk A, Mallory M, Wong J, Takenouchi T, Hashimoto M, Masliah E (2000) alpha-synuclein promotes mitochondrial deficit and oxidative stress. Am J Pathol 157: 401-410 – reference: Larsen KE, Schmitz Y, Troyer MD, Mosharov E, Dietrich P, Quazi AZ, Savalle M, Nemani V, Chaudhry FA, Edwards RH, Stefanis L, Sulzer D (2006) α-Synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis. J Neurosci 26: 11915-11922 – reference: Schullery SE, Schmidt CF, Felgner P, Tillack TW, Thompson TE (1980a) Fusion of dipalmitoylphosphatidylcholine vesicles. Biochemistry 19: 3919-3923 – reference: Haywood AF, Staveley BE (2006) Mutant alpha-synuclein-induced degeneration is reduced by parkin in a fly model of Parkinson's disease. Genome 49: 505-510 – reference: Hoppert M (2003) Microscopic Techniques in Biotechnology. Weinheim: Wiley-VCH – reference: Gitler AD, Chesi A, Geddie ML, Strathearn KE, Hamamichi S, Hill KJ, Caldwell KA, Caldwell GA, Cooper AA, Rochet JC, Lindquist S (2009) Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet 41: 308-315 – reference: Shavali S, Brown-Borg HM, Ebadi M, Porter J (2008) Mitochondrial localization of alpha-synuclein protein in alpha-synuclein overexpressing cells. Neurosci Lett 439: 125-128 – reference: Chernomordik LV, Kozlov MM (2003) Protein-lipid interplay in fusion and fission of biological membranes. Annu Rev Biochem 72: 175-207 – reference: Davidson SM, Yellon D, Duchen MR (2007) Assessing mitochondrial potential, calcium, and redox state in isolated mammalian cells using confocal microscopy. Methods Mol Biol 372: 421-430 – reference: Cho DH, Nakamura T, Lipton SA (2010) Mitochondrial dynamics in cell death and neurodegeneration. Cell Mol Life Sci (in press) – reference: Devi L, Raghavendran V, Prabhu BM, Avadhani NG, Anandatheerthavarada HK (2008) Mitochondrial import and accumulation of {alpha}-sy. J Biol Chem 283: 9089-9100 – reference: Lutz AK, Exner N, Fett ME, Schlehe JS, Kloos K, Laemmermann K, Brunner B, Kurz-Drexler A, Vogel F, Reichert AS, Bouman L, Vogt-Weisenhorn D, Wurst W, Tatzelt J, Haass C, Winklhofer KF (2009) Loss of parkin or PINK1 function increases DRP1-dependent mitochondrial fragmentation. J Biol Chem 284: 22938-22951 – reference: Tamm LK, Crane J, Kiessling V (2003) Membrane fusion: a structural perspective on the interplay of lipids and proteins. Curr Opin Struct Biol 13: 453-466 – reference: Martin LJ, Pan Y, Price AC, Sterling W, Copeland NG, Jenkins NA, Price DL, Lee MK (2006) Parkinson's disease alpha-synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death. J Neurosci 26: 41-50 – reference: Parihar MS, Parihar A, Fujita M, Hashimoto M, Ghafourifar P (2009) Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells. Int J Biochem Cell Biol 41: 2015-2024 – reference: Uversky VN (2007) Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation. J Neurochem 103: 17-37 – reference: Drescher M, Godschalk F, Veldhuis G, van Rooijen BD, Subramaniam V, Huber M (2008a) Spin-label EPR on alpha-synuclein reveals differences in the membrane binding affinity of the two antiparallel helices. Chembiochem 9: 2411-2416 – reference: Waak J, Weber SS, Gorner K, Schall C, Ichijo H, Stehle T, Kahle PJ (2009) Oxidizable residues mediating protein stability and cytoprotective interaction of DJ-1 with apoptosis signal-regulating kinase 1. J Biol Chem 284: 14245-14257 – reference: Lentz BR (2007) PEG as a tool to gain insight into membrane fusion. Eur Biophys J 36: 315-326 – reference: Simon-Sanchez J, Schulte C, Bras JM, Sharma M, Gibbs JR, Berg D, Paisan-Ruiz C, Lichtner P, Scholz SW, Hernandez DG, Kruger R, Federoff M, Klein C, Goate A, Perlmutter J, Bonin M, Nalls MA, Illig T, Gieger C, Houlden H et al (2009) Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nat Genet 41: 1308-1312 – reference: Kahle PJ, Neumann M, Ozmen L, Müller V, Odoy S, Okamoto N, Jacobsen H, Iwatsubo T, Trojanowski JQ, Takahashi H, Wakabayashi K, Bogdanovic N, Riederer P, Kreschmar HA, Haass C (2001) Selective insolubility of alpha-synuclein in human Lewy Body diseases is recapitulated in a transgenic mouse model. Am J Pathol 159: 2215-2225 – reference: Sharon R, Bar-Joseph I, Frosch MP, Walsh DM, Hamilton JA, Selkoe DJ (2003) The formation of highly soluble oligomers of α-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 37: 583-595 – reference: Kahle PJ, Neumann M, Ozmen L, Muller V, Jacobsen H, Schindzielorz A, Okochi M, Leimer U, van Der Putten H, Probst A, Kremmer E, Kretzschmar HA, Haass C (2000) Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha-synuclein in human and transgenic mouse brain. J Neurosci 20: 6365-6373 – reference: Lee JC, Langen R, Hummel PA, Gray HB, Winkler JR (2004b) Alpha-synuclein structures from fluorescence energy-transfer kinetics: implications for the role of the protein in Parkinson's disease. Proc Natl Acad Sci USA 101: 16466-16471 – reference: Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, Lee MJ, Chaudhry FA, Nicoli RA, Edwards RH (2010) Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65: 66-79 – reference: Beyer K (2007) Mechanistic aspects of Parkinson's disease. α-synuclein and the biomembrane. Cell Biochem Biophys 47: 285-299 – reference: Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M (1997) Alpha-synuclein in Lewy bodies. Nature 388: 839-840 – reference: Li WW, Yang R, Guo JC, Ren HM, Zha XL, Cheng JS, Cai DF (2007) Localization of alpha-synuclein to mitochondria within midbrain of mice. Neuroreport 18: 1543-1546 – reference: Struck DK, Hoekstra D, Pagano RE (1981) Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20: 4093-4099 – reference: Gorner K, Holtorf E, Odoy S, Nuscher B, Yamamoto A, Regula JT, Beyer K, Haass C, Kahle PJ (2004) Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1. J Biol Chem 279: 6943-6951 – reference: Chen X, Arac D, Wang TM, Gilpin CJ, Zimmerberg J, Rizo J (2006) SNARE-mediated lipid mixing depends on the physical state of the vesicles. Biophys J 90: 2062-2074 – reference: Palacino JJ, Sagi D, Goldberg MS, Krauss S, Motz C, Wacker M, Klose J, Shen J (2004) Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J Biol Chem 279: 18614-18622 – reference: Nickel W, Weber T, McNew JA, Parlati F, Sollner TH, Rothman JE (1999) Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc Natl Acad Sci USA 96: 12571-12576 – reference: Lei G, MacDonald RC (2003) Lipid bilayer vesicle fusion: intermediates captured by high-speed microfluorescence spectroscopy. Biophys J 85: 1585-1599 – reference: Singleton AB, Farrer M, Johnson J, Singleton A, Hague S, Kachergus J, Hulihan M, Peuralinna T, Dutra A, Nussbaum R, Lincoln S, Crawley A, Hanson M, Maraganore D, Adler C, Cookson MR, Muenter M, Baptista M, Miller D, Blancato J et al (2003) alpha-Synuclein locus triplication causes Parkinson's disease. Science 302: 841 – reference: Ibanez P, Bonnet AM, Debarges B, Lohmann E, Tison F, Pollak P, Agid Y, Durr A, Brice A (2004) Causal relation between alpha-synuclein gene duplication and familial Parkinson's disease. Lancet 364: 1169-1171 – reference: Satake W, Nakabayashi Y, Mizuta I, Hirota Y, Ito C, Kubo M, Kawaguchi T, Tsunoda T, Watanabe M, Takeda A, Tomiyama H, Nakashima K, Hasegawa K, Obata F, Yoshikawa T, Kawakami H, Sakoda S, Yamamoto M, Hattori N, Murata M et al (2009) Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nat Genet 41: 1303-1307 – reference: Todd AM, Staveley BE (2008) Pink1 suppresses alpha-synuclein-induced phenotypes in a Drosophila model of Parkinson's disease. Genome 51: 1040-1046 – reference: Gosavi N, Lee HJ, Lee JS, Patel S, Lee SJ (2002) Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J Biol Chem 277: 48984-48992 – reference: Harder Z, Zunino R, McBride H (2004) Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol 14: 340-345 – reference: Parihar MS, Parihar A, Fujita M, Hashimoto M, Ghafourifar P (2008) Mitochondrial association of alpha-synuclein causes oxidative stress. Cell Mol Life Sci 65: 1272-1284 – reference: Cole NB, Dieuliis D, Leo P, Mitchell DC, Nussbaum RL (2008) Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification. Exp Cell Res 314: 2076-2089 – reference: Lee HJ, Khoshaghideh F, Patel S, Lee SJ (2004a) Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. J Neurosci 24: 1888-1896 – reference: Canet-Aviles RM, Wilson MA, Miller DW, Ahmad R, McLendon C, Bandyopadhyay S, Baptista MJ, Ringe D, Petsko GA, Cookson MR (2004) The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc Natl Acad Sci USA 101: 9103-9108 – reference: Jo E, Darabie AA, Han K, Tandon A, Fraser PE, McLaurin J (2004) alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis. Eur J Biochem 271: 3180-3189 – reference: Jao CC, Hegde BG, Chen J, Haworth IS, Langen R (2008) Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement. Proc Natl Acad Sci USA 105: 19666-19671 – reference: Bodner CR, Dobson CM, Bax A (2009) Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy. J Mol Biol 390: 775-790 – reference: Iwai A, Masliah E, Yoshimoto M, Ge N, Flanagan L, de Silva HA, Kittel A, Saitoh T (1995) The precursor protein of non-A beta component of Alzheimer′s disease amyloid is a presynaptic protein of the central nervous system. Neuron 14: 467-475 – reference: Rostaing P, Weimer RM, Jorgensen EM, Triller A, Bessereau JL (2004) Preservation of immunoreactivity and fine structure of adult C. elegans tissues using high-pressure freezing. J Histochem Cytochem 52: 1-12 – reference: Ferreon AC, Gambin Y, Lemke EA, Deniz AA (2009) Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. Proc Natl Acad Sci USA 106: 5645-5650 – reference: Ulmer TS, Bax A (2005) Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants. J Biol Chem 280: 43179-43187 – reference: Ramakrishnan M, Jensen PH, Marsh D (2006) Association of alpha-synuclein and mutants with lipid membranes: spin-label ESR and polarized IR. Biochemistry 45: 3386-3395 – reference: Reynolds ES (1963) The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol 17: 208-212 – reference: Yavich L, Tanila H, Vepsalainen S, Jakala P (2004) Role of alpha-synuclein in presynaptic dopamine recruitment. J Neurosci 24: 11165-11170 – reference: Uversky VN (2002) What does it mean to be natively unfolded? Eur J Biochem 269: 2-12 – reference: Kim RH, Smith PD, Aleyasin H, Hayley S, Mount MP, Pownall S, Wakeham A, You-Ten AJ, Kalia SK, Horne P, Westaway D, Lozano AM, Anisman H, Park DS, Mak TW (2005) Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc Natl Acad Sci USA 102: 5215-5220 – reference: Wood-Kaczmar A, Gandhi S, Yao Z, Abramov AY, Miljan EA, Keen G, Stanyer L, Hargreaves I, Klupsch K, Deas E, Downward J, Mansfield L, Jat P, Taylor J, Heales S, Duchen MR, Latchman D, Tabrizi SJ, Wood NW (2008) PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons. PLoS One 3: e2455 – reference: Fujita Y, Ohama E, Takatama M, Al-Sarraj S, Okamoto K (2006) Fragmentation of Golgi apparatus of nigral neurons with alpha-synuclein-positive inclusions in patients with Parkinson's disease. Acta Neuropathol 112: 261-265 – reference: Grundemann J, Schlaudraff F, Haeckel O, Liss B (2008) Elevated alpha-synuclein mRNA levels in individual UV-laser-microdissected dopaminergic substantia nigra neurons in idiopathic Parkinson's disease. Nucleic Acids Res 36: e38 – reference: Niemann A, Ruegg M, La Padula V, Schenone A, Suter U (2005) Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease. J Cell Biol 170: 1067-1078 – reference: Detmer SA, Chan DC (2007) Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 8: 870-879 – reference: Ben Gedalya T, Loeb V, Israeli E, Altschuler Y, Selkoe DJ, Sharon R (2009) Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling. Traffic 10: 218-234 – reference: Cornell RB, Taneva SG (2006) Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Curr Protein Pept Sci 7: 539-552 – reference: Trexler A, Rhoades E (2009) α-Synuclein binds large unilamellar vesicles as an extended helix. Biochemistry 48: 2304-2306 – reference: Okita C, Sato M, Schroeder T (2004) Generation of optimized yellow and red fluorescent proteins with distinct subcellular localization. Biotechniques 36: 418-422, 424 – reference: Exner N, Treske B, Paquet D, Holmstrom K, Schiesling C, Gispert S, Carballo-Carbajal I, Berg D, Hoepken HH, Gasser T, Kruger R, Winklhofer KF, Vogel F, Reichert AS, Auburger G, Kahle PJ, Schmid B, Haass C (2007) Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J Neurosci 27: 12413-12418 – reference: Chen M, Margittai M, Chen J, Langen R (2007) Investigation of alpha-synuclein fibril structure by site-directed spin labeling. J Biol Chem 282: 24970-24979 – reference: Derksen A, Gantz D, Small DM (1996) Calorimetry of apolipoprotein-A1 binding to phosphatidylcholine-triolein-cholesterol emulsions. Biophys J 70: 330-338 – reference: Tsika E, Moysidou M, Guo J, Cushman M, Gannon P, Sandaltzopoulos R, Giasson BI, Krainc D, Ischiropoulos H, Mazzulli JR (2010) Distinct region-specific alpha-synuclein oligomers in A53T transgenic mice: implications for neurodegeneration. J Neurosci 30: 3409-3418 – reference: Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, Minoshima S, Yokochi M, Mizuno Y, Shimizu N (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-608 – reference: Drescher M, Veldhuis G, van Rooijen BD, Milikisyants S, Subramaniam V, Huber M (2008b) Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein. J Am Chem Soc 130: 7796-7797 – reference: Takamori S, Holt M, Stenius K, Lemke EA, Gronborg M, Riedel D, Urlaub H, Schenck S, Brugger B, Ringler P, Muller SA, Rammner B, Grater F, Hub JS, De Groot BL, Mieskes G, Moriyama Y, Klingauf J, Grubmuller H, Heuser J et al (2006) Molecular anatomy of a trafficking organelle. Cell 127: 831-846 – reference: Kayed R, Pensalfini A, Margol L, Sokolov Y, Sarsoza F, Head E, Hall J, Glabe C (2009) Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. J Biol Chem 284: 4230-4237 – reference: Schullery SE, Schmidt CF, Felgner P, Tillack TW, Thompson TE (1980b) Fusion of dipalmitoylphosphatidylcholine vesicles. Biochemistry 19: 3919-3923 – reference: Davidson WS, Jonas A, Clayton DF, George JM (1998) Stabilization of α-synuclein secondary structue upon bindung to synthetic membranes. J Biol Chem 273: 9443-9449 – reference: Hasegawa T, Matsuzaki M, Takeda A, Kikuchi A, Akita H, Perry G, Smith MA, Itoyama Y (2004) Accelerated alpha-synuclein aggregation after differentiation of SH-SY5Y neuroblastoma cells. Brain Res 1013: 51-59 – reference: Gursky O (2005) Apolipoprotein structure and dynamics. Curr Opin Lipidol 16: 287-294 – reference: Lee HJ, Khoshaghideh F, Lee S, Lee SJ (2006) Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein. Eur J Neurosci 24: 3153-3162 – reference: Chiba-Falek O, Lopez GJ, Nussbaum RL (2006) Levels of alpha-synuclein mRNA in sporadic Parkinson disease patients. Mov Disord 21: 1703-1708 – reference: Kamp F, Beyer K (2006) Binding of α-synuclein affects the lipid packing in bilayers of small vesicles. J Biol Chem 281: 9251-9259 – reference: Malka F, Aure K, Goffart S, Spelbrink JN, Rojo M (2007) The mitochondria of cultured mammalian cells: I. Analysis by immunofluorescence microscopy, histochemistry, subcellular fractionation, and cell fusion. Methods Mol Biol 372: 3-16 – reference: Ulmer TS, Bax A, Cole NB, Nussbaum RL (2005) Structure and dynamics of micelle-bound human alpha-synuclein. J Biol Chem 280: 9595-9603 – reference: Park J, Lee SB, Lee S, Kim Y, Song S, Kim S, Bae E, Kim J, Shong M, Kim JM, Chung J (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441: 1157-1161 – reference: Jensen PH, Nielsen MS, Jakes R, Dotti CG, Goedert M (1998) Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J Biol Chem 273: 26292-26294 – reference: Haque ME, McIntosh TJ, Lentz BR (2001) Influence of lipid composition on physical properties and PEG-mediated fusion of curved and uncurved model membrane vesicles: 'nature's own fusogenic lipid bilayer'. Biochemistry 40: 4340-4348 – reference: Westermann B (2008) Molecular machinery of mitochondrial fusion and fission. J Biol Chem 283: 13501-13505 – reference: Chandra S, Fornai F, Kwon HB, Yazdani U, Atasoy D, Liu X, Hammer RE, Battaglia G, German DC, Castillo PE, Sudhof TC (2004) Double-knockout mice for alpha- and beta-synucleins: effect on synaptic functions. Proc Natl Acad Sci USA 101: 14966-14971 – reference: Dagda RK, Cherra III SJ, Kulich SM, Tandon A, Park D, Chu CT (2009) Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem 284: 13843-13855 – reference: Giannakis E, Pacifico J, Smith DP, Hung LW, Masters CL, Cappai R, Wade JD, Barnham KJ (2008) Dimeric structures of alpha-synuclein bind preferentially to lipid membranes. Biochim Biophys Acta 1778: 1112-1119 – reference: Gaber BP, Sheridan JP (1982) Kinetic and thermodynamic studies of the fusion of small unilamellar phospholipid vesicles. Biochim Biophys Acta 685: 87-93 – reference: Mello CC, Kramer JM, Stinchcomb D, Ambros V (1991) Efficient gene transfer in C. elegans: extrachromosomal maintenance and integration of transforming sequences. EMBO J 10: 3959-3970 – reference: Abeliovich A, Schmitz Y, Farinas I, Choi-Lundberg D, Ho WH, Castillo PE, Shinsky N, Verdugo JM, Armanini M, Ryan A, Hynes M, Phillips H, Sulzer D, Rosenthal A (2000) Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 25: 239-252 – reference: Chandra S, Gallardo G, Fernandez-Chacon R, Schluter OM, Sudhof TC (2005) Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell 123: 383-396 – reference: Henn IH, Gostner JM, Lackner P, Tatzelt J, Winklhofer KF (2005) Pathogenic mutations inactivate parkin by distinct mechanisms. J Neurochem 92: 114-122 – reference: Henn IH, Bouman L, Schlehe JS, Schlierf A, Schramm JE, Wegener E, Nakaso K, Culmsee C, Berninger B, Krappmann D, Tatzelt J, Winklhofer KF (2007) Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J Neurosci 27: 1868-1878 – reference: Herndon LA, Schmeissner PJ, Dudaronek JM, Brown PA, Listner KM, Sakano Y, Paupard MC, Hall DH, Driscoll M (2002) Stochastic and genetic factors influence tissue-specific decline in ageing C. elegans. Nature 419: 808-814 – reference: Dennison SM, Bowen ME, Brunger AT, Lentz BR (2006) Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion. Biophys J 90: 1661-1675 – reference: Labrousse AM, Zappaterra MD, Rube DA, VanderBliek AM (1999) C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane. Mol Cell 4: 815-826 – reference: Maroteaux L, Campanelli JT, Scheller RH (1988) Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J Neurosci 8: 2804-2815 – reference: Pantazatos DP, MacDonald RC (1999) Directly observed membrane fusion between oppositely charged phospholipid bilayers. J Membr Biol 170: 27-38 – reference: Clark IE, Dodson MW, Jiang C, Cao JH, Huh JR, Seol JH, Yoo SJ, Hay BA, Guo M (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441: 1162-1166 – reference: Cabin DE, Shimazu K, Murphy D, Cole NB, Gottschalk W, McIlwain KL, Orrison B, Chen A, Ellis CE, Paylor R, Lu B, Nussbaum RL (2002) Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J Neurosci 22: 8797-8807 – reference: Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998) SNAREpins: minimal machinery for membrane fusion. Cell 92: 759-772 – reference: Ishihara N, Jofuku A, Eura Y, Mihara K (2003) Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells. Biochem Biophys Res Commun 301: 891-898 – reference: Smith WW, Jiang H, Pei Z, Tanaka Y, Morita H, Sawa A, Dawson VL, Dawson TM, Ross CA (2005) Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum Mol Genet 14: 3801-3811 – reference: Geisler S, Holmstrom KM, Skujat D, Fiesel FC, Rothfuss OC, Kahle PJ, Springer W (2010) PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat Cell Biol 12: 119-131 – reference: Neuspiel M, Zunino R, Gangaraju S, Rippstein P, McBride H (2005) Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization. J Biol Chem 280: 25060-25070 – reference: Maraganore DM, de Andrade M, Elbaz A, Farrer MJ, Ioannidis JP, Kruger R, Rocca WA, Schneider NK, Lesnick TG, Lincoln SJ, Hulihan MM, Aasly JO, Ashizawa T, Chartier-Harlin MC, Checkoway H, Ferrarese C, Hadjigeorgiou G, Hattori N, Kawakami H, Lambert JC et al (2006) Collaborative analysis of alpha-synuclein gene promoter variability and Parkinson disease. JAMA 296: 661-670 – volume: 24 start-page: 1888 year: 2004 end-page: 1896 ident: CR72 article-title: Clearance of alpha‐synuclein oligomeric intermediates via the lysosomal degradation pathway publication-title: J Neurosci – volume: 364 start-page: 1169 year: 2004 end-page: 1171 ident: CR54 article-title: Causal relation between alpha‐synuclein gene duplication and familial Parkinson's disease publication-title: Lancet – volume: 1778 start-page: 1112 year: 2008 end-page: 1119 ident: CR36 article-title: Dimeric structures of alpha‐synuclein bind preferentially to lipid membranes publication-title: Biochim Biophys Acta – volume: 37 start-page: 583 year: 2003 end-page: 595 ident: CR108 article-title: The formation of highly soluble oligomers of α‐synuclein is regulated by fatty acids and enhanced in Parkinson's disease publication-title: Neuron – volume: 441 start-page: 1162 year: 2006 end-page: 1166 ident: CR15 article-title: Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin publication-title: Nature – volume: 281 start-page: 9251 year: 2006 end-page: 9259 ident: CR62 article-title: Binding of α‐synuclein affects the lipid packing in bilayers of small vesicles publication-title: J Biol Chem – volume: 14 start-page: 467 year: 1995 end-page: 475 ident: CR56 article-title: The precursor protein of non‐A beta component of Alzheimer′s disease amyloid is a presynaptic protein of the central nervous system publication-title: Neuron – volume: 282 start-page: 24970 year: 2007 end-page: 24979 ident: CR9 article-title: Investigation of alpha‐synuclein fibril structure by site‐directed spin labeling publication-title: J Biol Chem – volume: 313 start-page: 324 year: 2006 end-page: 328 ident: CR17 article-title: Alpha‐synuclein blocks ER‐Golgi traffic and Rab1 rescues neuron loss in Parkinson's models publication-title: Science – volume: 1193 start-page: 219 year: 1994 end-page: 225 ident: CR134 article-title: Calorimetric studies of the interactions of cytochrome c with dioleoylphosphatidylglycerol extruded vesicles: ionic strength effects publication-title: Biochim Biophys Acta – volume: 302 start-page: 841 year: 2003 ident: CR111 article-title: alpha‐Synuclein locus triplication causes Parkinson's disease publication-title: Science – volume: 51 start-page: 1040 year: 2008 end-page: 1046 ident: CR117 article-title: Pink1 suppresses alpha‐synuclein‐induced phenotypes in a Drosophila model of Parkinson's disease publication-title: Genome – volume: 281 start-page: 37972 year: 2006 end-page: 37979 ident: CR30 article-title: Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology publication-title: J Biol Chem – volume: 273 start-page: 26292 year: 1998 end-page: 26294 ident: CR58 article-title: Binding of alpha‐synuclein to brain vesicles is abolished by familial Parkinson's disease mutation publication-title: J Biol Chem – volume: 146 start-page: 1 year: 1995 end-page: 14 ident: CR11 article-title: Lipids in biological membrane fusion publication-title: J Membr Biol – volume: 101 start-page: 16466 year: 2004 end-page: 16471 ident: CR73 article-title: Alpha‐synuclein structures from fluorescence energy‐transfer kinetics: implications for the role of the protein in Parkinson's disease publication-title: Proc Natl Acad Sci USA – volume: 280 start-page: 43179 year: 2005 end-page: 43187 ident: CR120 article-title: Comparison of structure and dynamics of micelle‐bound human alpha‐synuclein and Parkinson disease variants publication-title: J Biol Chem – volume: 36 start-page: e38 year: 2008 ident: CR42 article-title: Elevated alpha‐synuclein mRNA levels in individual UV‐laser‐microdissected dopaminergic substantia nigra neurons in idiopathic Parkinson's disease publication-title: Nucleic Acids Res – volume: 28 start-page: 12305 year: 2008 end-page: 12317 ident: CR86 article-title: Optical reporters for the conformation of alpha‐synuclein reveal a specific interaction with mitochondria publication-title: J Neurosci – volume: 159 start-page: 2215 year: 2001 end-page: 2225 ident: CR61 article-title: Selective insolubility of alpha‐synuclein in human Lewy Body diseases is recapitulated in a transgenic mouse model publication-title: Am J Pathol – volume: 304 start-page: 1158 year: 2004 end-page: 1160 ident: CR124 article-title: Hereditary early‐onset Parkinson's disease caused by mutations in PINK1 publication-title: Science – volume: 296 start-page: 661 year: 2006 end-page: 670 ident: CR80 article-title: Collaborative analysis of alpha‐synuclein gene promoter variability and Parkinson disease publication-title: JAMA – volume: 170 start-page: 1067 year: 2005 end-page: 1078 ident: CR90 article-title: Ganglioside‐induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot‐Marie‐Tooth disease publication-title: J Cell Biol – volume: 14 start-page: 3801 year: 2005 end-page: 3811 ident: CR112 article-title: Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha‐synuclein‐induced toxicity publication-title: Hum Mol Genet – volume: 279 start-page: 18614 year: 2004 end-page: 18622 ident: CR94 article-title: Mitochondrial dysfunction and oxidative damage in parkin‐deficient mice publication-title: J Biol Chem – volume: 105 start-page: 19666 year: 2008 end-page: 19671 ident: CR57 article-title: Structure of membrane‐bound alpha‐synuclein from site‐directed spin labeling and computational refinement publication-title: Proc Natl Acad Sci USA – volume: 14 start-page: 340 year: 2004 end-page: 345 ident: CR46 article-title: Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission publication-title: Curr Biol – volume: 12 start-page: 119 year: 2010 end-page: 131 ident: CR35 article-title: PINK1/Parkin‐mediated mitophagy is dependent on VDAC1 and p62/SQSTM1 publication-title: Nat Cell Biol – volume: 25 start-page: 239 year: 2000 end-page: 252 ident: CR1 article-title: Mice lacking alpha‐synuclein display functional deficits in the nigrostriatal dopamine system publication-title: Neuron – volume: 101 start-page: 14966 year: 2004 end-page: 14971 ident: CR7 article-title: Double‐knockout mice for alpha‐ and beta‐synucleins: effect on synaptic functions publication-title: Proc Natl Acad Sci USA – volume: 314 start-page: 2076 year: 2008 end-page: 2089 ident: CR16 article-title: Mitochondrial translocation of alpha‐synuclein is promoted by intracellular acidification publication-title: Exp Cell Res – volume: 284 start-page: 4230 year: 2009 end-page: 4237 ident: CR64 article-title: Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer publication-title: J Biol Chem – volume: 102 start-page: 5215 year: 2005 end-page: 5220 ident: CR65 article-title: Hypersensitivity of DJ‐1‐deficient mice to 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyrindine (MPTP) and oxidative stress publication-title: Proc Natl Acad Sci USA – volume: 13 start-page: 453 year: 2003 end-page: 466 ident: CR116 article-title: Membrane fusion: a structural perspective on the interplay of lipids and proteins publication-title: Curr Opin Struct Biol – volume: 27 start-page: 12413 year: 2007 end-page: 12418 ident: CR31 article-title: Loss‐of‐function of human PINK1 results in mitochondrial pathology and can be rescued by parkin publication-title: J Neurosci – volume: 7 start-page: 539 year: 2006 end-page: 552 ident: CR18 article-title: Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties publication-title: Curr Protein Pept Sci – volume: 21 start-page: 21966 year: 2004 end-page: 21975 ident: CR91 article-title: α‐synuclein has a high affinity for packing defects in a bilayer membrane. A thermodynamics study publication-title: J Biol Chem – volume: 439 start-page: 125 year: 2008 end-page: 128 ident: CR109 article-title: Mitochondrial localization of alpha‐synuclein protein in alpha‐synuclein overexpressing cells publication-title: Neurosci Lett – volume: 157 start-page: 401 year: 2000 end-page: 410 ident: CR53 article-title: alpha‐synuclein promotes mitochondrial deficit and oxidative stress publication-title: Am J Pathol – volume: 390 start-page: 775 year: 2009 end-page: 790 ident: CR4 article-title: Multiple tight phospholipid‐binding modes of alpha‐synuclein revealed by solution NMR spectroscopy publication-title: J Mol Biol – volume: 20 start-page: 4093 year: 1981 end-page: 4099 ident: CR114 article-title: Use of resonance energy transfer to monitor membrane fusion publication-title: Biochemistry – volume: 4 start-page: e5701 year: 2009 ident: CR104 article-title: Mitochondrial alterations in PINK1 deficient cells are influenced by calcineurin‐dependent dephosphorylation of dynamin‐related protein 1 publication-title: PLoS One – volume: 685 start-page: 87 year: 1982 end-page: 93 ident: CR34 article-title: Kinetic and thermodynamic studies of the fusion of small unilamellar phospholipid vesicles publication-title: Biochim Biophys Acta – volume: 92 start-page: 114 year: 2005 end-page: 122 ident: CR50 article-title: Pathogenic mutations inactivate parkin by distinct mechanisms publication-title: J Neurochem – volume: 112 start-page: 261 year: 2006 end-page: 265 ident: CR33 article-title: Fragmentation of Golgi apparatus of nigral neurons with alpha‐synuclein‐positive inclusions in patients with Parkinson's disease publication-title: Acta Neuropathol – volume: 170 start-page: 27 year: 1999 end-page: 38 ident: CR95 article-title: Directly observed membrane fusion between oppositely charged phospholipid bilayers publication-title: J Membr Biol – volume: 4 start-page: 815 year: 1999 end-page: 826 ident: CR69 article-title: C. elegans dynamin‐related protein DRP‐1 controls severing of the mitochondrial outer membrane publication-title: Mol Cell – volume: 8 start-page: 743 year: 2007 end-page: 754 ident: CR100 article-title: A neuroscientist's guide to lipidomics publication-title: Nat Rev – ident: CR52 – volume: 52 start-page: 1 year: 2004 end-page: 12 ident: CR103 article-title: Preservation of immunoreactivity and fine structure of adult C. elegans tissues using high‐pressure freezing publication-title: J Histochem Cytochem – volume: 30 start-page: 3409 year: 2010 end-page: 3418 ident: CR119 article-title: Distinct region‐specific alpha‐synuclein oligomers in A53T transgenic mice: implications for neurodegeneration publication-title: J Neurosci – volume: 90 start-page: 1661 year: 2006 end-page: 1675 ident: CR22 article-title: Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG‐mediated membrane fusion publication-title: Biophys J – volume: 10 start-page: 3959 year: 1991 end-page: 3970 ident: CR83 article-title: Efficient gene transfer in C. elegans: extrachromosomal maintenance and integration of transforming sequences publication-title: EMBO J – volume: 17 start-page: 208 year: 1963 end-page: 212 ident: CR102 article-title: The use of lead citrate at high pH as an electron‐opaque stain in electron microscopy publication-title: J Cell Biol – volume: 19 start-page: 3919 year: 1980 end-page: 3923 ident: CR106 article-title: Fusion of dipalmitoylphosphatidylcholine vesicles publication-title: Biochemistry – volume: 22 start-page: 8797 year: 2002 end-page: 8807 ident: CR5 article-title: Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha‐synuclein publication-title: J Neurosci – volume: 372 start-page: 421 year: 2007 end-page: 430 ident: CR20 article-title: Assessing mitochondrial potential, calcium, and redox state in isolated mammalian cells using confocal microscopy publication-title: Methods Mol Biol – volume: 41 start-page: 308 year: 2009 end-page: 315 ident: CR38 article-title: Alpha‐synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity publication-title: Nat Genet – volume: 20 start-page: 3214 year: 2000 end-page: 3220 ident: CR85 article-title: Synucleins are developmentally expressed, and alpha‐synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons publication-title: J Neurosci – volume: 372 start-page: 3 year: 2007 end-page: 16 ident: CR79 article-title: The mitochondria of cultured mammalian cells: I. Analysis by immunofluorescence microscopy, histochemistry, subcellular fractionation, and cell fusion publication-title: Methods Mol Biol – volume: 283 start-page: 13501 year: 2008 end-page: 13505 ident: CR129 article-title: Molecular machinery of mitochondrial fusion and fission publication-title: J Biol Chem – volume: 89 start-page: 2458 year: 2005 end-page: 2472 ident: CR77 article-title: SNARE‐driven, 25‐millisecond vesicle fusion publication-title: Biophys J – volume: 273 start-page: 9443 year: 1998 end-page: 9449 ident: CR21 article-title: Stabilization of α‐synuclein secondary structue upon bindung to synthetic membranes publication-title: J Biol Chem – volume: 280 start-page: 25060 year: 2005 end-page: 25070 ident: CR88 article-title: Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization publication-title: J Biol Chem – volume: 271 start-page: 3180 year: 2004 end-page: 3189 ident: CR59 article-title: alpha‐Synuclein‐synaptosomal membrane interactions: implications for fibrillogenesis publication-title: Eur J Biochem – volume: 8 start-page: 101 year: 2007 end-page: 112 ident: CR44 article-title: Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer′s amyloid beta‐peptide publication-title: Nat Rev Mol Cell Biol – volume: 45 start-page: 3386 year: 2006 end-page: 3395 ident: CR101 article-title: Association of alpha‐synuclein and mutants with lipid membranes: spin‐label ESR and polarized IR publication-title: Biochemistry – volume: 92 start-page: 4012 year: 2007 end-page: 4029 ident: CR128 article-title: Analysis of membrane fusion as a two‐state sequential process: evaluation of the stalk model publication-title: Biophys J – volume: 20 start-page: 6365 year: 2000 end-page: 6373 ident: CR60 article-title: Subcellular localization of wild‐type and Parkinson's disease‐associated mutant alpha‐synuclein in human and transgenic mouse brain publication-title: J Neurosci – volume: 65 start-page: 66 year: 2010 end-page: 79 ident: CR87 article-title: Increased expression of alpha‐synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis publication-title: Neuron – volume: 24 start-page: 3153 year: 2006 end-page: 3162 ident: CR71 article-title: Impairment of microtubule‐dependent trafficking by overexpression of alpha‐synuclein publication-title: Eur J Neurosci – volume: 9 start-page: 2411 year: 2008 end-page: 2416 ident: CR28 article-title: Spin‐label EPR on alpha‐synuclein reveals differences in the membrane binding affinity of the two antiparallel helices publication-title: Chembiochem – volume: 130 start-page: 7796 year: 2008 end-page: 7797 ident: CR29 article-title: Antiparallel arrangement of the helices of vesicle‐bound alpha‐synuclein publication-title: J Am Chem Soc – volume: 278 start-page: 37530 year: 2003 end-page: 37535 ident: CR23 article-title: Structural organization of α‐synuclein fibrils studied by site‐directed spin labeling publication-title: J Biol Chem – volume: 28 start-page: 3256 year: 2009 end-page: 3268 ident: CR63 article-title: Pre‐fibrillar alpha‐synuclein variants with impaired beta‐structure increase neurotoxicity in Parkinson's disease models publication-title: EMBO J – volume: 282 start-page: 13680 year: 2007 end-page: 13691 ident: CR40 article-title: Structural determinants of the C‐terminal helix‐kink‐helix motif essential for protein stability and survival promoting activity of DJ‐1 publication-title: J Biol Chem – volume: 103 start-page: 17 year: 2007 end-page: 37 ident: CR123 article-title: Neuropathology, biochemistry, and biophysics of alpha‐synuclein aggregation publication-title: J Neurochem – volume: 16 start-page: 287 year: 2005 end-page: 294 ident: CR43 article-title: Apolipoprotein structure and dynamics publication-title: Curr Opin Lipidol – volume: 26 start-page: 41 year: 2006 end-page: 50 ident: CR82 article-title: Parkinson's disease alpha‐synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death publication-title: J Neurosci – volume: 49 start-page: 505 year: 2006 end-page: 510 ident: CR48 article-title: Mutant alpha‐synuclein‐induced degeneration is reduced by parkin in a fly model of Parkinson's disease publication-title: Genome – volume: 19 start-page: 3919 year: 1980 end-page: 3923 ident: CR107 article-title: Fusion of dipalmitoylphosphatidylcholine vesicles publication-title: Biochemistry – volume: 48 start-page: 2304 year: 2009 end-page: 2306 ident: CR118 article-title: α‐Synuclein binds large unilamellar vesicles as an extended helix publication-title: Biochemistry – volume: 283 start-page: 10992 year: 2008 end-page: 11003 ident: CR67 article-title: Single‐particle characterization of iron‐induced pore‐forming alpha ‐synuclein oligomers publication-title: J Biol Chem – volume: 40 start-page: 4340 year: 2001 end-page: 4348 ident: CR45 article-title: Influence of lipid composition on physical properties and PEG‐mediated fusion of curved and uncurved model membrane vesicles: ‘nature's own fusogenic lipid bilayer’ publication-title: Biochemistry – volume: 41 start-page: 1308 year: 2009 end-page: 1312 ident: CR110 article-title: Genome‐wide association study reveals genetic risk underlying Parkinson's disease publication-title: Nat Genet – volume: 388 start-page: 839 year: 1997 end-page: 840 ident: CR113 article-title: Alpha‐synuclein in Lewy bodies publication-title: Nature – volume: 392 start-page: 605 year: 1998 end-page: 608 ident: CR66 article-title: Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism publication-title: Nature – volume: 1980 start-page: 6011 year: 1980 end-page: 6021 ident: CR130 article-title: Studies on the mechanism of membrane fusion: kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicles contents publication-title: Biochemistry – volume: 351 start-page: 29 year: 2003 end-page: 32 ident: CR93 article-title: Alpha‐synuclein expression in HEK293 cells enhances the mitochondrial sensitivity to rotenone publication-title: Neurosci Lett – volume: 395 start-page: 627 year: 2010 end-page: 642 ident: CR125 article-title: Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha‐synuclein aggregation publication-title: J Mol Biol – volume: 278 start-page: 47199 year: 2003 end-page: 47208 ident: CR131 article-title: Inactivation of parkin by oxidative stress and C‐terminal truncations: a protective role of molecular chaperones publication-title: J Biol Chem – volume: 106 start-page: 5645 year: 2009 end-page: 5650 ident: CR32 article-title: Interplay of alpha‐synuclein binding and conformational switching probed by single‐molecule fluorescence publication-title: Proc Natl Acad Sci USA – volume: 65 start-page: 1272 year: 2008 end-page: 1284 ident: CR96 article-title: Mitochondrial association of alpha‐synuclein causes oxidative stress publication-title: Cell Mol Life Sci – volume: 85 start-page: 1585 year: 2003 end-page: 1599 ident: CR74 article-title: Lipid bilayer vesicle fusion: intermediates captured by high‐speed microfluorescence spectroscopy publication-title: Biophys J – volume: 283 start-page: 9089 year: 2008 end-page: 9100 ident: CR26 article-title: Mitochondrial import and accumulation of {alpha}‐sy publication-title: J Biol Chem – volume: 41 start-page: 2015 year: 2009 end-page: 2024 ident: CR97 article-title: Alpha‐synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells publication-title: Int J Biochem Cell Biol – volume: 127 start-page: 831 year: 2006 end-page: 846 ident: CR115 article-title: Molecular anatomy of a trafficking organelle publication-title: Cell – volume: 27 start-page: 1405 year: 2007 end-page: 1410 ident: CR68 article-title: Presynaptic alpha‐synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies publication-title: J Neurosci – volume: 96 start-page: 12571 year: 1999 end-page: 12576 ident: CR89 article-title: Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v‐SNAREs and t‐SNAREs publication-title: Proc Natl Acad Sci USA – volume: 41 start-page: 1303 year: 2009 end-page: 1307 ident: CR105 article-title: Genome‐wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease publication-title: Nat Genet – volume: 21 start-page: 1703 year: 2006 end-page: 1708 ident: CR13 article-title: Levels of alpha‐synuclein mRNA in sporadic Parkinson disease patients publication-title: Mov Disord – volume: 1 start-page: 99 year: 2009 end-page: 111 ident: CR84 article-title: Parkinson's disease mutations in PINK1 result in decreased complex I activity and deficient synaptic function publication-title: EMBO Mol Med – volume: 18 start-page: 1543 year: 2007 end-page: 1546 ident: CR76 article-title: Localization of alpha‐synuclein to mitochondria within midbrain of mice publication-title: Neuroreport – volume: 277 start-page: 48984 year: 2002 end-page: 48992 ident: CR41 article-title: Golgi fragmentation occurs in the cells with prefibrillar alpha‐synuclein aggregates and precedes the formation of fibrillar inclusion publication-title: J Biol Chem – volume: 3 start-page: e2455 year: 2008 ident: CR132 article-title: PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons publication-title: PLoS One – ident: CR14 – volume: 1013 start-page: 51 year: 2004 end-page: 59 ident: CR47 article-title: Accelerated alpha‐synuclein aggregation after differentiation of SH‐SY5Y neuroblastoma cells publication-title: Brain Res – volume: 301 start-page: 891 year: 2003 end-page: 898 ident: CR55 article-title: Regulation of mitochondrial morphology by membrane potential, and DRP1‐dependent division and FZO1‐dependent fusion reaction in mammalian cells publication-title: Biochem Biophys Res Commun – volume: 269 start-page: 2 year: 2002 end-page: 12 ident: CR122 article-title: What does it mean to be natively unfolded? publication-title: Eur J Biochem – volume: 284 start-page: 7177 year: 2009 end-page: 7189 ident: CR99 article-title: Curvature dynamics of α‐synuclein familial Parkinson disease mutants: molecular simulations of the micelle‐ and bilayer‐bound forms publication-title: J Biol Chem – volume: 279 start-page: 6943 year: 2004 end-page: 6951 ident: CR39 article-title: Differential effects of Parkinson's disease‐associated mutations on stability and folding of DJ‐1 publication-title: J Biol Chem – volume: 24 start-page: 11165 year: 2004 end-page: 11170 ident: CR133 article-title: Role of alpha‐synuclein in presynaptic dopamine recruitment publication-title: J Neurosci – volume: 90 start-page: 2062 year: 2006 end-page: 2074 ident: CR10 article-title: SNARE‐mediated lipid mixing depends on the physical state of the vesicles publication-title: Biophys J – volume: 280 start-page: 9595 year: 2005 end-page: 9603 ident: CR121 article-title: Structure and dynamics of micelle‐bound human alpha‐synuclein publication-title: J Biol Chem – volume: 441 start-page: 1157 year: 2006 end-page: 1161 ident: CR98 article-title: Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin publication-title: Nature – volume: 101 start-page: 9103 year: 2004 end-page: 9108 ident: CR6 article-title: The Parkinson's disease protein DJ‐1 is neuroprotective due to cysteine‐sulfinic acid‐driven mitochondrial localization publication-title: Proc Natl Acad Sci USA – volume: 426 start-page: 884 year: 2003 end-page: 890 ident: CR27 article-title: Protein folding and misfolding publication-title: Nature – volume: 8 start-page: 2804 year: 1988 end-page: 2815 ident: CR81 article-title: Synuclein: a neuron‐specific protein localized to the nucleus and presynaptic nerve terminal publication-title: J Neurosci – volume: 105 start-page: 145 year: 2008 end-page: 150 ident: CR37 article-title: The Parkinson's disease protein alpha‐synuclein disrupts cellular Rab homeostasis publication-title: Proc Natl Acad Sci USA – volume: 36 start-page: 315 year: 2007 end-page: 326 ident: CR75 article-title: PEG as a tool to gain insight into membrane fusion publication-title: Eur Biophys J – volume: 26 start-page: 11915 year: 2006 end-page: 11922 ident: CR70 article-title: α‐Synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis publication-title: J Neurosci – volume: 92 start-page: 759 year: 1998 end-page: 772 ident: CR127 article-title: SNAREpins: minimal machinery for membrane fusion publication-title: Cell – volume: 10 start-page: 218 year: 2009 end-page: 234 ident: CR2 article-title: Alpha‐synuclein and polyunsaturated fatty acids promote clathrin‐mediated endocytosis and synaptic vesicle recycling publication-title: Traffic – volume: 8 start-page: 870 year: 2007 end-page: 879 ident: CR25 article-title: Functions and dysfunctions of mitochondrial dynamics publication-title: Nat Rev Mol Cell Biol – volume: 36 start-page: 418 year: 2004 end-page: 422 ident: CR92 article-title: Generation of optimized yellow and red fluorescent proteins with distinct subcellular localization publication-title: Biotechniques – volume: 72 start-page: 175 year: 2003 end-page: 207 ident: CR12 article-title: Protein‐lipid interplay in fusion and fission of biological membranes publication-title: Annu Rev Biochem – volume: 47 start-page: 285 year: 2007 end-page: 299 ident: CR3 article-title: Mechanistic aspects of Parkinson's disease. α‐synuclein and the biomembrane publication-title: Cell Biochem Biophys – volume: 70 start-page: 330 year: 1996 end-page: 338 ident: CR24 article-title: Calorimetry of apolipoprotein‐A1 binding to phosphatidylcholine‐triolein‐cholesterol emulsions publication-title: Biophys J – volume: 27 start-page: 1868 year: 2007 end-page: 1878 ident: CR49 article-title: Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor‐kappaB signaling publication-title: J Neurosci – volume: 284 start-page: 14245 year: 2009 end-page: 14257 ident: CR126 article-title: Oxidizable residues mediating protein stability and cytoprotective interaction of DJ‐1 with apoptosis signal‐regulating kinase 1 publication-title: J Biol Chem – volume: 419 start-page: 808 year: 2002 end-page: 814 ident: CR51 article-title: Stochastic and genetic factors influence tissue‐specific decline in ageing C. elegans publication-title: Nature – volume: 123 start-page: 383 year: 2005 end-page: 396 ident: CR8 article-title: Alpha‐synuclein cooperates with CSPalpha in preventing neurodegeneration publication-title: Cell – volume: 284 start-page: 13843 year: 2009 end-page: 13855 ident: CR19 article-title: Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission publication-title: J Biol Chem – volume: 284 start-page: 22938 year: 2009 end-page: 22951 ident: CR78 article-title: Loss of parkin or PINK1 function increases DRP1‐dependent mitochondrial fragmentation publication-title: J Biol Chem – volume: 17 start-page: 208 year: 1963 end-page: 212 article-title: The use of lead citrate at high pH as an electron‐opaque stain in electron microscopy publication-title: J Cell Biol – volume: 4 start-page: 815 year: 1999 end-page: 826 article-title: C. elegans dynamin‐related protein DRP‐1 controls severing of the mitochondrial outer membrane publication-title: Mol Cell – volume: 284 start-page: 14245 year: 2009 end-page: 14257 article-title: Oxidizable residues mediating protein stability and cytoprotective interaction of DJ‐1 with apoptosis signal‐regulating kinase 1 publication-title: J Biol Chem – volume: 7 start-page: 539 year: 2006 end-page: 552 article-title: Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties publication-title: Curr Protein Pept Sci – volume: 284 start-page: 4230 year: 2009 end-page: 4237 article-title: Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer publication-title: J Biol Chem – volume: 390 start-page: 775 year: 2009 end-page: 790 article-title: Multiple tight phospholipid‐binding modes of alpha‐synuclein revealed by solution NMR spectroscopy publication-title: J Mol Biol – volume: 72 start-page: 175 year: 2003 end-page: 207 article-title: Protein‐lipid interplay in fusion and fission of biological membranes publication-title: Annu Rev Biochem – volume: 102 start-page: 5215 year: 2005 end-page: 5220 article-title: Hypersensitivity of DJ‐1‐deficient mice to 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyrindine (MPTP) and oxidative stress publication-title: Proc Natl Acad Sci USA – volume: 283 start-page: 10992 year: 2008 end-page: 11003 article-title: Single‐particle characterization of iron‐induced pore‐forming alpha ‐synuclein oligomers publication-title: J Biol Chem – volume: 48 start-page: 2304 year: 2009 end-page: 2306 article-title: α‐Synuclein binds large unilamellar vesicles as an extended helix publication-title: Biochemistry – volume: 96 start-page: 12571 year: 1999 end-page: 12576 article-title: Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v‐SNAREs and t‐SNAREs publication-title: Proc Natl Acad Sci USA – volume: 28 start-page: 3256 year: 2009 end-page: 3268 article-title: Pre‐fibrillar alpha‐synuclein variants with impaired beta‐structure increase neurotoxicity in Parkinson's disease models publication-title: EMBO J – volume: 27 start-page: 1405 year: 2007 end-page: 1410 article-title: Presynaptic alpha‐synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies publication-title: J Neurosci – volume: 103 start-page: 17 year: 2007 end-page: 37 article-title: Neuropathology, biochemistry, and biophysics of alpha‐synuclein aggregation publication-title: J Neurochem – volume: 9 start-page: 2411 year: 2008a end-page: 2416 article-title: Spin‐label EPR on alpha‐synuclein reveals differences in the membrane binding affinity of the two antiparallel helices publication-title: Chembiochem – volume: 16 start-page: 287 year: 2005 end-page: 294 article-title: Apolipoprotein structure and dynamics publication-title: Curr Opin Lipidol – volume: 392 start-page: 605 year: 1998 end-page: 608 article-title: Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism publication-title: Nature – volume: 3 start-page: e2455 year: 2008 article-title: PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons publication-title: PLoS One – volume: 284 start-page: 13843 year: 2009 end-page: 13855 article-title: Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission publication-title: J Biol Chem – volume: 280 start-page: 9595 year: 2005 end-page: 9603 article-title: Structure and dynamics of micelle‐bound human alpha‐synuclein publication-title: J Biol Chem – volume: 24 start-page: 3153 year: 2006 end-page: 3162 article-title: Impairment of microtubule‐dependent trafficking by overexpression of alpha‐synuclein publication-title: Eur J Neurosci – year: 2010 article-title: Mitochondrial dynamics in cell death and neurodegeneration publication-title: Cell Mol Life Sci – volume: 101 start-page: 9103 year: 2004 end-page: 9108 article-title: The Parkinson's disease protein DJ‐1 is neuroprotective due to cysteine‐sulfinic acid‐driven mitochondrial localization publication-title: Proc Natl Acad Sci USA – volume: 13 start-page: 453 year: 2003 end-page: 466 article-title: Membrane fusion: a structural perspective on the interplay of lipids and proteins publication-title: Curr Opin Struct Biol – volume: 92 start-page: 114 year: 2005 end-page: 122 article-title: Pathogenic mutations inactivate parkin by distinct mechanisms publication-title: J Neurochem – volume: 284 start-page: 7177 year: 2009 end-page: 7189 article-title: Curvature dynamics of α‐synuclein familial Parkinson disease mutants: molecular simulations of the micelle‐ and bilayer‐bound forms publication-title: J Biol Chem – volume: 20 start-page: 4093 year: 1981 end-page: 4099 article-title: Use of resonance energy transfer to monitor membrane fusion publication-title: Biochemistry – volume: 146 start-page: 1 year: 1995 end-page: 14 article-title: Lipids in biological membrane fusion publication-title: J Membr Biol – volume: 278 start-page: 47199 year: 2003 end-page: 47208 article-title: Inactivation of parkin by oxidative stress and C‐terminal truncations: a protective role of molecular chaperones publication-title: J Biol Chem – volume: 26 start-page: 11915 year: 2006 end-page: 11922 article-title: α‐Synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis publication-title: J Neurosci – volume: 101 start-page: 16466 year: 2004b end-page: 16471 article-title: Alpha‐synuclein structures from fluorescence energy‐transfer kinetics: implications for the role of the protein in Parkinson's disease publication-title: Proc Natl Acad Sci USA – volume: 101 start-page: 14966 year: 2004 end-page: 14971 article-title: Double‐knockout mice for alpha‐ and beta‐synucleins: effect on synaptic functions publication-title: Proc Natl Acad Sci USA – volume: 65 start-page: 1272 year: 2008 end-page: 1284 article-title: Mitochondrial association of alpha‐synuclein causes oxidative stress publication-title: Cell Mol Life Sci – volume: 4 start-page: e5701 year: 2009 article-title: Mitochondrial alterations in PINK1 deficient cells are influenced by calcineurin‐dependent dephosphorylation of dynamin‐related protein 1 publication-title: PLoS One – volume: 14 start-page: 3801 year: 2005 end-page: 3811 article-title: Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha‐synuclein‐induced toxicity publication-title: Hum Mol Genet – volume: 441 start-page: 1162 year: 2006 end-page: 1166 article-title: Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin publication-title: Nature – volume: 92 start-page: 4012 year: 2007 end-page: 4029 article-title: Analysis of membrane fusion as a two‐state sequential process: evaluation of the stalk model publication-title: Biophys J – volume: 90 start-page: 1661 year: 2006 end-page: 1675 article-title: Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG‐mediated membrane fusion publication-title: Biophys J – volume: 170 start-page: 1067 year: 2005 end-page: 1078 article-title: Ganglioside‐induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot‐Marie‐Tooth disease publication-title: J Cell Biol – volume: 27 start-page: 1868 year: 2007 end-page: 1878 article-title: Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor‐kappaB signaling publication-title: J Neurosci – volume: 14 start-page: 340 year: 2004 end-page: 345 article-title: Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission publication-title: Curr Biol – volume: 89 start-page: 2458 year: 2005 end-page: 2472 article-title: SNARE‐driven, 25‐millisecond vesicle fusion publication-title: Biophys J – volume: 296 start-page: 661 year: 2006 end-page: 670 article-title: Collaborative analysis of alpha‐synuclein gene promoter variability and Parkinson disease publication-title: JAMA – volume: 314 start-page: 2076 year: 2008 end-page: 2089 article-title: Mitochondrial translocation of alpha‐synuclein is promoted by intracellular acidification publication-title: Exp Cell Res – volume: 284 start-page: 22938 year: 2009 end-page: 22951 article-title: Loss of parkin or PINK1 function increases DRP1‐dependent mitochondrial fragmentation publication-title: J Biol Chem – volume: 41 start-page: 2015 year: 2009 end-page: 2024 article-title: Alpha‐synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells publication-title: Int J Biochem Cell Biol – volume: 70 start-page: 330 year: 1996 end-page: 338 article-title: Calorimetry of apolipoprotein‐A1 binding to phosphatidylcholine‐triolein‐cholesterol emulsions publication-title: Biophys J – volume: 1 start-page: 99 year: 2009 end-page: 111 article-title: Parkinson's disease mutations in PINK1 result in decreased complex I activity and deficient synaptic function publication-title: EMBO Mol Med – volume: 36 start-page: 418 year: 2004 end-page: 422 article-title: Generation of optimized yellow and red fluorescent proteins with distinct subcellular localization publication-title: Biotechniques – volume: 1980 start-page: 6011 year: 1980 end-page: 6021 article-title: Studies on the mechanism of membrane fusion: kinetics of calcium ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicles contents publication-title: Biochemistry – volume: 273 start-page: 9443 year: 1998 end-page: 9449 article-title: Stabilization of α‐synuclein secondary structue upon bindung to synthetic membranes publication-title: J Biol Chem – volume: 273 start-page: 26292 year: 1998 end-page: 26294 article-title: Binding of alpha‐synuclein to brain vesicles is abolished by familial Parkinson's disease mutation publication-title: J Biol Chem – volume: 419 start-page: 808 year: 2002 end-page: 814 article-title: Stochastic and genetic factors influence tissue‐specific decline in ageing C. elegans publication-title: Nature – volume: 112 start-page: 261 year: 2006 end-page: 265 article-title: Fragmentation of Golgi apparatus of nigral neurons with alpha‐synuclein‐positive inclusions in patients with Parkinson's disease publication-title: Acta Neuropathol – volume: 439 start-page: 125 year: 2008 end-page: 128 article-title: Mitochondrial localization of alpha‐synuclein protein in alpha‐synuclein overexpressing cells publication-title: Neurosci Lett – volume: 159 start-page: 2215 year: 2001 end-page: 2225 article-title: Selective insolubility of alpha‐synuclein in human Lewy Body diseases is recapitulated in a transgenic mouse model publication-title: Am J Pathol – volume: 313 start-page: 324 year: 2006 end-page: 328 article-title: Alpha‐synuclein blocks ER‐Golgi traffic and Rab1 rescues neuron loss in Parkinson's models publication-title: Science – volume: 395 start-page: 627 year: 2010 end-page: 642 article-title: Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha‐synuclein aggregation publication-title: J Mol Biol – volume: 22 start-page: 8797 year: 2002 end-page: 8807 article-title: Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha‐synuclein publication-title: J Neurosci – volume: 351 start-page: 29 year: 2003 end-page: 32 article-title: Alpha‐synuclein expression in HEK293 cells enhances the mitochondrial sensitivity to rotenone publication-title: Neurosci Lett – volume: 52 start-page: 1 year: 2004 end-page: 12 article-title: Preservation of immunoreactivity and fine structure of adult C. elegans tissues using high‐pressure freezing publication-title: J Histochem Cytochem – volume: 372 start-page: 3 year: 2007 end-page: 16 article-title: The mitochondria of cultured mammalian cells: I. Analysis by immunofluorescence microscopy, histochemistry, subcellular fractionation, and cell fusion publication-title: Methods Mol Biol – volume: 364 start-page: 1169 year: 2004 end-page: 1171 article-title: Causal relation between alpha‐synuclein gene duplication and familial Parkinson's disease publication-title: Lancet – volume: 388 start-page: 839 year: 1997 end-page: 840 article-title: Alpha‐synuclein in Lewy bodies publication-title: Nature – volume: 49 start-page: 505 year: 2006 end-page: 510 article-title: Mutant alpha‐synuclein‐induced degeneration is reduced by parkin in a fly model of Parkinson's disease publication-title: Genome – volume: 157 start-page: 401 year: 2000 end-page: 410 article-title: alpha‐synuclein promotes mitochondrial deficit and oxidative stress publication-title: Am J Pathol – volume: 30 start-page: 3409 year: 2010 end-page: 3418 article-title: Distinct region‐specific alpha‐synuclein oligomers in A53T transgenic mice: implications for neurodegeneration publication-title: J Neurosci – volume: 123 start-page: 383 year: 2005 end-page: 396 article-title: Alpha‐synuclein cooperates with CSPalpha in preventing neurodegeneration publication-title: Cell – volume: 282 start-page: 13680 year: 2007 end-page: 13691 article-title: Structural determinants of the C‐terminal helix‐kink‐helix motif essential for protein stability and survival promoting activity of DJ‐1 publication-title: J Biol Chem – volume: 20 start-page: 3214 year: 2000 end-page: 3220 article-title: Synucleins are developmentally expressed, and alpha‐synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons publication-title: J Neurosci – volume: 1013 start-page: 51 year: 2004 end-page: 59 article-title: Accelerated alpha‐synuclein aggregation after differentiation of SH‐SY5Y neuroblastoma cells publication-title: Brain Res – volume: 21 start-page: 21966 year: 2004 end-page: 21975 article-title: α‐synuclein has a high affinity for packing defects in a bilayer membrane. A thermodynamics study publication-title: J Biol Chem – volume: 282 start-page: 24970 year: 2007 end-page: 24979 article-title: Investigation of alpha‐synuclein fibril structure by site‐directed spin labeling publication-title: J Biol Chem – volume: 18 start-page: 1543 year: 2007 end-page: 1546 article-title: Localization of alpha‐synuclein to mitochondria within midbrain of mice publication-title: Neuroreport – volume: 85 start-page: 1585 year: 2003 end-page: 1599 article-title: Lipid bilayer vesicle fusion: intermediates captured by high‐speed microfluorescence spectroscopy publication-title: Biophys J – volume: 8 start-page: 743 year: 2007 end-page: 754 article-title: A neuroscientist's guide to lipidomics publication-title: Nat Rev – volume: 280 start-page: 43179 year: 2005 end-page: 43187 article-title: Comparison of structure and dynamics of micelle‐bound human alpha‐synuclein and Parkinson disease variants publication-title: J Biol Chem – volume: 47 start-page: 285 year: 2007 end-page: 299 article-title: Mechanistic aspects of Parkinson's disease. α‐synuclein and the biomembrane publication-title: Cell Biochem Biophys – volume: 127 start-page: 831 year: 2006 end-page: 846 article-title: Molecular anatomy of a trafficking organelle publication-title: Cell – volume: 10 start-page: 218 year: 2009 end-page: 234 article-title: Alpha‐synuclein and polyunsaturated fatty acids promote clathrin‐mediated endocytosis and synaptic vesicle recycling publication-title: Traffic – volume: 372 start-page: 421 year: 2007 end-page: 430 article-title: Assessing mitochondrial potential, calcium, and redox state in isolated mammalian cells using confocal microscopy publication-title: Methods Mol Biol – volume: 27 start-page: 12413 year: 2007 end-page: 12418 article-title: Loss‐of‐function of human PINK1 results in mitochondrial pathology and can be rescued by parkin publication-title: J Neurosci – volume: 8 start-page: 101 year: 2007 end-page: 112 article-title: Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer′s amyloid beta‐peptide publication-title: Nat Rev Mol Cell Biol – volume: 36 start-page: 315 year: 2007 end-page: 326 article-title: PEG as a tool to gain insight into membrane fusion publication-title: Eur Biophys J – volume: 92 start-page: 759 year: 1998 end-page: 772 article-title: SNAREpins: minimal machinery for membrane fusion publication-title: Cell – volume: 90 start-page: 2062 year: 2006 end-page: 2074 article-title: SNARE‐mediated lipid mixing depends on the physical state of the vesicles publication-title: Biophys J – volume: 45 start-page: 3386 year: 2006 end-page: 3395 article-title: Association of alpha‐synuclein and mutants with lipid membranes: spin‐label ESR and polarized IR publication-title: Biochemistry – volume: 302 start-page: 841 year: 2003 article-title: alpha‐Synuclein locus triplication causes Parkinson's disease publication-title: Science – volume: 1193 start-page: 219 year: 1994 end-page: 225 article-title: Calorimetric studies of the interactions of cytochrome c with dioleoylphosphatidylglycerol extruded vesicles: ionic strength effects publication-title: Biochim Biophys Acta – year: 2003 publication-title: Microscopic Techniques in Biotechnology – volume: 280 start-page: 25060 year: 2005 end-page: 25070 article-title: Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization publication-title: J Biol Chem – volume: 279 start-page: 18614 year: 2004 end-page: 18622 article-title: Mitochondrial dysfunction and oxidative damage in parkin‐deficient mice publication-title: J Biol Chem – volume: 37 start-page: 583 year: 2003 end-page: 595 article-title: The formation of highly soluble oligomers of α‐synuclein is regulated by fatty acids and enhanced in Parkinson's disease publication-title: Neuron – volume: 283 start-page: 13501 year: 2008 end-page: 13505 article-title: Molecular machinery of mitochondrial fusion and fission publication-title: J Biol Chem – volume: 269 start-page: 2 year: 2002 end-page: 12 article-title: What does it mean to be natively unfolded? publication-title: Eur J Biochem – volume: 283 start-page: 9089 year: 2008 end-page: 9100 article-title: Mitochondrial import and accumulation of {alpha}‐sy publication-title: J Biol Chem – volume: 41 start-page: 1303 year: 2009 end-page: 1307 article-title: Genome‐wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease publication-title: Nat Genet – volume: 685 start-page: 87 year: 1982 end-page: 93 article-title: Kinetic and thermodynamic studies of the fusion of small unilamellar phospholipid vesicles publication-title: Biochim Biophys Acta – volume: 271 start-page: 3180 year: 2004 end-page: 3189 article-title: alpha‐Synuclein‐synaptosomal membrane interactions: implications for fibrillogenesis publication-title: Eur J Biochem – volume: 65 start-page: 66 year: 2010 end-page: 79 article-title: Increased expression of alpha‐synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis publication-title: Neuron – volume: 304 start-page: 1158 year: 2004 end-page: 1160 article-title: Hereditary early‐onset Parkinson's disease caused by mutations in PINK1 publication-title: Science – volume: 8 start-page: 2804 year: 1988 end-page: 2815 article-title: Synuclein: a neuron‐specific protein localized to the nucleus and presynaptic nerve terminal publication-title: J Neurosci – volume: 40 start-page: 4340 year: 2001 end-page: 4348 article-title: Influence of lipid composition on physical properties and PEG‐mediated fusion of curved and uncurved model membrane vesicles: ‘nature's own fusogenic lipid bilayer’ publication-title: Biochemistry – volume: 24 start-page: 1888 year: 2004a end-page: 1896 article-title: Clearance of alpha‐synuclein oligomeric intermediates via the lysosomal degradation pathway publication-title: J Neurosci – volume: 8 start-page: 870 year: 2007 end-page: 879 article-title: Functions and dysfunctions of mitochondrial dynamics publication-title: Nat Rev Mol Cell Biol – volume: 26 start-page: 41 year: 2006 end-page: 50 article-title: Parkinson's disease alpha‐synuclein transgenic mice develop neuronal mitochondrial degeneration and cell death publication-title: J Neurosci – volume: 426 start-page: 884 year: 2003 end-page: 890 article-title: Protein folding and misfolding publication-title: Nature – volume: 51 start-page: 1040 year: 2008 end-page: 1046 article-title: Pink1 suppresses alpha‐synuclein‐induced phenotypes in a Drosophila model of Parkinson's disease publication-title: Genome – volume: 277 start-page: 48984 year: 2002 end-page: 48992 article-title: Golgi fragmentation occurs in the cells with prefibrillar alpha‐synuclein aggregates and precedes the formation of fibrillar inclusion publication-title: J Biol Chem – volume: 12 start-page: 119 year: 2010 end-page: 131 article-title: PINK1/Parkin‐mediated mitophagy is dependent on VDAC1 and p62/SQSTM1 publication-title: Nat Cell Biol – volume: 24 start-page: 11165 year: 2004 end-page: 11170 article-title: Role of alpha‐synuclein in presynaptic dopamine recruitment publication-title: J Neurosci – volume: 106 start-page: 5645 year: 2009 end-page: 5650 article-title: Interplay of alpha‐synuclein binding and conformational switching probed by single‐molecule fluorescence publication-title: Proc Natl Acad Sci USA – volume: 21 start-page: 1703 year: 2006 end-page: 1708 article-title: Levels of alpha‐synuclein mRNA in sporadic Parkinson disease patients publication-title: Mov Disord – volume: 278 start-page: 37530 year: 2003 end-page: 37535 article-title: Structural organization of α‐synuclein fibrils studied by site‐directed spin labeling publication-title: J Biol Chem – volume: 14 start-page: 467 year: 1995 end-page: 475 article-title: The precursor protein of non‐A beta component of Alzheimer′s disease amyloid is a presynaptic protein of the central nervous system publication-title: Neuron – volume: 170 start-page: 27 year: 1999 end-page: 38 article-title: Directly observed membrane fusion between oppositely charged phospholipid bilayers publication-title: J Membr Biol – volume: 105 start-page: 145 year: 2008 end-page: 150 article-title: The Parkinson's disease protein alpha‐synuclein disrupts cellular Rab homeostasis publication-title: Proc Natl Acad Sci USA – volume: 301 start-page: 891 year: 2003 end-page: 898 article-title: Regulation of mitochondrial morphology by membrane potential, and DRP1‐dependent division and FZO1‐dependent fusion reaction in mammalian cells publication-title: Biochem Biophys Res Commun – volume: 20 start-page: 6365 year: 2000 end-page: 6373 article-title: Subcellular localization of wild‐type and Parkinson's disease‐associated mutant alpha‐synuclein in human and transgenic mouse brain publication-title: J Neurosci – volume: 41 start-page: 1308 year: 2009 end-page: 1312 article-title: Genome‐wide association study reveals genetic risk underlying Parkinson's disease publication-title: Nat Genet – volume: 10 start-page: 3959 year: 1991 end-page: 3970 article-title: Efficient gene transfer in C. elegans: extrachromosomal maintenance and integration of transforming sequences publication-title: EMBO J – volume: 36 start-page: e38 year: 2008 article-title: Elevated alpha‐synuclein mRNA levels in individual UV‐laser‐microdissected dopaminergic substantia nigra neurons in idiopathic Parkinson's disease publication-title: Nucleic Acids Res – volume: 41 start-page: 308 year: 2009 end-page: 315 article-title: Alpha‐synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity publication-title: Nat Genet – volume: 279 start-page: 6943 year: 2004 end-page: 6951 article-title: Differential effects of Parkinson's disease‐associated mutations on stability and folding of DJ‐1 publication-title: J Biol Chem – volume: 25 start-page: 239 year: 2000 end-page: 252 article-title: Mice lacking alpha‐synuclein display functional deficits in the nigrostriatal dopamine system publication-title: Neuron – volume: 28 start-page: 12305 year: 2008 end-page: 12317 article-title: Optical reporters for the conformation of alpha‐synuclein reveal a specific interaction with mitochondria publication-title: J Neurosci – volume: 281 start-page: 9251 year: 2006 end-page: 9259 article-title: Binding of α‐synuclein affects the lipid packing in bilayers of small vesicles publication-title: J Biol Chem – volume: 281 start-page: 37972 year: 2006 end-page: 37979 article-title: Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology publication-title: J Biol Chem – volume: 441 start-page: 1157 year: 2006 end-page: 1161 article-title: Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin publication-title: Nature – volume: 130 start-page: 7796 year: 2008b end-page: 7797 article-title: Antiparallel arrangement of the helices of vesicle‐bound alpha‐synuclein publication-title: J Am Chem Soc – volume: 1778 start-page: 1112 year: 2008 end-page: 1119 article-title: Dimeric structures of alpha‐synuclein bind preferentially to lipid membranes publication-title: Biochim Biophys Acta – volume: 19 start-page: 3919 year: 1980a end-page: 3923 article-title: Fusion of dipalmitoylphosphatidylcholine vesicles publication-title: Biochemistry – volume: 105 start-page: 19666 year: 2008 end-page: 19671 article-title: Structure of membrane‐bound alpha‐synuclein from site‐directed spin labeling and computational refinement publication-title: Proc Natl Acad Sci USA – volume: 19 start-page: 3919 year: 1980b end-page: 3923 article-title: Fusion of dipalmitoylphosphatidylcholine vesicles publication-title: Biochemistry – volume: 92 start-page: 759 year: 1998 ident: emboj2010223-b127 publication-title: Cell doi: 10.1016/S0092-8674(00)81404-X – volume: 170 start-page: 1067 year: 2005 ident: emboj2010223-b90 publication-title: J Cell Biol doi: 10.1083/jcb.200507087 – volume: 269 start-page: 2 year: 2002 ident: emboj2010223-b122 publication-title: Eur J Biochem doi: 10.1046/j.0014-2956.2001.02649.x – volume: 90 start-page: 1661 year: 2006 ident: emboj2010223-b22 publication-title: Biophys J doi: 10.1529/biophysj.105.069617 – volume: 18 start-page: 1543 year: 2007 ident: emboj2010223-b76 publication-title: Neuroreport doi: 10.1097/WNR.0b013e3282f03db4 – volume: 372 start-page: 3 year: 2007 ident: emboj2010223-b79 publication-title: Methods Mol Biol doi: 10.1007/978-1-59745-365-3_1 – volume: 65 start-page: 66 year: 2010 ident: emboj2010223-b87 publication-title: Neuron doi: 10.1016/j.neuron.2009.12.023 – volume: 92 start-page: 114 year: 2005 ident: emboj2010223-b50 publication-title: J Neurochem doi: 10.1111/j.1471-4159.2004.02854.x – volume: 52 start-page: 1 year: 2004 ident: emboj2010223-b103 publication-title: J Histochem Cytochem doi: 10.1177/002215540405200101 – volume: 14 start-page: 467 year: 1995 ident: emboj2010223-b56 publication-title: Neuron doi: 10.1016/0896-6273(95)90302-X – volume: 1013 start-page: 51 year: 2004 ident: emboj2010223-b47 publication-title: Brain Res doi: 10.1016/j.brainres.2004.04.018 – volume: 284 start-page: 4230 year: 2009 ident: emboj2010223-b64 publication-title: J Biol Chem doi: 10.1074/jbc.M808591200 – volume: 36 start-page: 418 year: 2004 ident: emboj2010223-b92 publication-title: Biotechniques doi: 10.2144/04363ST01 – volume: 70 start-page: 330 year: 1996 ident: emboj2010223-b24 publication-title: Biophys J doi: 10.1016/S0006-3495(96)79574-7 – volume: 17 start-page: 208 year: 1963 ident: emboj2010223-b102 publication-title: J Cell Biol doi: 10.1083/jcb.17.1.208 – volume: 41 start-page: 1308 year: 2009 ident: emboj2010223-b110 publication-title: Nat Genet doi: 10.1038/ng.487 – volume: 25 start-page: 239 year: 2000 ident: emboj2010223-b1 publication-title: Neuron doi: 10.1016/S0896-6273(00)80886-7 – volume: 21 start-page: 1703 year: 2006 ident: emboj2010223-b13 publication-title: Mov Disord doi: 10.1002/mds.21007 – volume: 282 start-page: 13680 year: 2007 ident: emboj2010223-b40 publication-title: J Biol Chem doi: 10.1074/jbc.M609821200 – volume: 30 start-page: 3409 year: 2010 ident: emboj2010223-b119 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.4977-09.2010 – volume: 20 start-page: 3214 year: 2000 ident: emboj2010223-b85 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.20-09-03214.2000 – volume: 282 start-page: 24970 year: 2007 ident: emboj2010223-b9 publication-title: J Biol Chem doi: 10.1074/jbc.M700368200 – volume: 426 start-page: 884 year: 2003 ident: emboj2010223-b27 publication-title: Nature doi: 10.1038/nature02261 – volume: 157 start-page: 401 year: 2000 ident: emboj2010223-b53 publication-title: Am J Pathol doi: 10.1016/S0002-9440(10)64553-1 – volume: 280 start-page: 43179 year: 2005 ident: emboj2010223-b120 publication-title: J Biol Chem doi: 10.1074/jbc.M507624200 – volume: 1 start-page: 99 year: 2009 ident: emboj2010223-b84 publication-title: EMBO Mol Med doi: 10.1002/emmm.200900006 – volume: 22 start-page: 8797 year: 2002 ident: emboj2010223-b5 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.22-20-08797.2002 – volume: 277 start-page: 48984 year: 2002 ident: emboj2010223-b41 publication-title: J Biol Chem doi: 10.1074/jbc.M208194200 – volume: 284 start-page: 13843 year: 2009 ident: emboj2010223-b19 publication-title: J Biol Chem doi: 10.1074/jbc.M808515200 – volume: 10 start-page: 3959 year: 1991 ident: emboj2010223-b83 publication-title: EMBO J doi: 10.1002/j.1460-2075.1991.tb04966.x – volume: 96 start-page: 12571 year: 1999 ident: emboj2010223-b89 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.96.22.12571 – volume: 112 start-page: 261 year: 2006 ident: emboj2010223-b33 publication-title: Acta Neuropathol doi: 10.1007/s00401-006-0114-4 – volume: 40 start-page: 4340 year: 2001 ident: emboj2010223-b45 publication-title: Biochemistry doi: 10.1021/bi002030k – volume: 123 start-page: 383 year: 2005 ident: emboj2010223-b8 publication-title: Cell doi: 10.1016/j.cell.2005.09.028 – volume: 390 start-page: 775 year: 2009 ident: emboj2010223-b4 publication-title: J Mol Biol doi: 10.1016/j.jmb.2009.05.066 – volume: 388 start-page: 839 year: 1997 ident: emboj2010223-b113 publication-title: Nature doi: 10.1038/42166 – volume: 24 start-page: 1888 year: 2004a ident: emboj2010223-b72 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.3809-03.2004 – volume: 280 start-page: 25060 year: 2005 ident: emboj2010223-b88 publication-title: J Biol Chem doi: 10.1074/jbc.M501599200 – volume: 89 start-page: 2458 year: 2005 ident: emboj2010223-b77 publication-title: Biophys J doi: 10.1529/biophysj.105.062539 – volume: 12 start-page: 119 year: 2010 ident: emboj2010223-b35 publication-title: Nat Cell Biol doi: 10.1038/ncb2012 – volume: 392 start-page: 605 year: 1998 ident: emboj2010223-b66 publication-title: Nature doi: 10.1038/33416 – volume: 101 start-page: 16466 year: 2004b ident: emboj2010223-b73 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0407307101 – volume: 7 start-page: 539 year: 2006 ident: emboj2010223-b18 publication-title: Curr Protein Pept Sci doi: 10.2174/138920306779025675 – volume: 10 start-page: 218 year: 2009 ident: emboj2010223-b2 publication-title: Traffic doi: 10.1111/j.1600-0854.2008.00853.x – volume: 273 start-page: 26292 year: 1998 ident: emboj2010223-b58 publication-title: J Biol Chem doi: 10.1074/jbc.273.41.26292 – volume: 26 start-page: 41 year: 2006 ident: emboj2010223-b82 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.4308-05.2006 – volume: 441 start-page: 1162 year: 2006 ident: emboj2010223-b15 publication-title: Nature doi: 10.1038/nature04779 – volume: 296 start-page: 661 year: 2006 ident: emboj2010223-b80 publication-title: JAMA doi: 10.1001/jama.296.6.661 – volume: 8 start-page: 743 year: 2007 ident: emboj2010223-b100 publication-title: Nat Rev doi: 10.1038/nrn2233 – volume: 4 start-page: 815 year: 1999 ident: emboj2010223-b69 publication-title: Mol Cell doi: 10.1016/S1097-2765(00)80391-3 – volume: 105 start-page: 145 year: 2008 ident: emboj2010223-b37 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0710685105 – volume: 395 start-page: 627 year: 2010 ident: emboj2010223-b125 publication-title: J Mol Biol doi: 10.1016/j.jmb.2009.10.066 – volume: 313 start-page: 324 year: 2006 ident: emboj2010223-b17 publication-title: Science doi: 10.1126/science.1129462 – volume: 281 start-page: 9251 year: 2006 ident: emboj2010223-b62 publication-title: J Biol Chem doi: 10.1074/jbc.M512292200 – volume: 4 start-page: e5701 year: 2009 ident: emboj2010223-b104 publication-title: PLoS One doi: 10.1371/journal.pone.0005701 – volume: 27 start-page: 1405 year: 2007 ident: emboj2010223-b68 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.4564-06.2007 – volume: 85 start-page: 1585 year: 2003 ident: emboj2010223-b74 publication-title: Biophys J doi: 10.1016/S0006-3495(03)74590-1 – volume: 47 start-page: 285 year: 2007 ident: emboj2010223-b3 publication-title: Cell Biochem Biophys doi: 10.1007/s12013-007-0014-9 – volume: 280 start-page: 9595 year: 2005 ident: emboj2010223-b121 publication-title: J Biol Chem doi: 10.1074/jbc.M411805200 – volume: 20 start-page: 6365 year: 2000 ident: emboj2010223-b60 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.20-17-06365.2000 – volume: 127 start-page: 831 year: 2006 ident: emboj2010223-b115 publication-title: Cell doi: 10.1016/j.cell.2006.10.030 – volume: 9 start-page: 2411 year: 2008a ident: emboj2010223-b28 publication-title: Chembiochem doi: 10.1002/cbic.200800238 – volume: 14 start-page: 3801 year: 2005 ident: emboj2010223-b112 publication-title: Hum Mol Genet doi: 10.1093/hmg/ddi396 – volume: 49 start-page: 505 year: 2006 ident: emboj2010223-b48 publication-title: Genome doi: 10.1139/g06-011 – volume: 101 start-page: 9103 year: 2004 ident: emboj2010223-b6 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0402959101 – volume: 278 start-page: 37530 year: 2003 ident: emboj2010223-b23 publication-title: J Biol Chem doi: 10.1074/jbc.M305266200 – volume: 159 start-page: 2215 year: 2001 ident: emboj2010223-b61 publication-title: Am J Pathol doi: 10.1016/S0002-9440(10)63072-6 – volume: 41 start-page: 308 year: 2009 ident: emboj2010223-b38 publication-title: Nat Genet doi: 10.1038/ng.300 – volume: 48 start-page: 2304 year: 2009 ident: emboj2010223-b118 publication-title: Biochemistry doi: 10.1021/bi900114z – volume: 283 start-page: 10992 year: 2008 ident: emboj2010223-b67 publication-title: J Biol Chem doi: 10.1074/jbc.M709634200 – volume: 16 start-page: 287 year: 2005 ident: emboj2010223-b43 publication-title: Curr Opin Lipidol doi: 10.1097/01.mol.0000169348.61191.ac – volume: 8 start-page: 870 year: 2007 ident: emboj2010223-b25 publication-title: Nat Rev Mol Cell Biol doi: 10.1038/nrm2275 – volume: 102 start-page: 5215 year: 2005 ident: emboj2010223-b65 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0501282102 – volume: 284 start-page: 7177 year: 2009 ident: emboj2010223-b99 publication-title: J Biol Chem doi: 10.1074/jbc.M808895200 – volume: 41 start-page: 1303 year: 2009 ident: emboj2010223-b105 publication-title: Nat Genet doi: 10.1038/ng.485 – volume: 284 start-page: 22938 year: 2009 ident: emboj2010223-b78 publication-title: J Biol Chem doi: 10.1074/jbc.M109.035774 – volume: 283 start-page: 9089 year: 2008 ident: emboj2010223-b26 publication-title: J Biol Chem doi: 10.1074/jbc.M710012200 – volume: 351 start-page: 29 year: 2003 ident: emboj2010223-b93 publication-title: Neurosci Lett doi: 10.1016/S0304-3940(03)00941-8 – volume: 314 start-page: 2076 year: 2008 ident: emboj2010223-b16 publication-title: Exp Cell Res doi: 10.1016/j.yexcr.2008.03.012 – volume: 51 start-page: 1040 year: 2008 ident: emboj2010223-b117 publication-title: Genome doi: 10.1139/G08-085 – volume: 146 start-page: 1 year: 1995 ident: emboj2010223-b11 publication-title: J Membr Biol doi: 10.1007/BF00232676 – volume: 1980 start-page: 6011 year: 1980 ident: emboj2010223-b130 publication-title: Biochemistry doi: 10.1021/bi00567a011 – volume: 283 start-page: 13501 year: 2008 ident: emboj2010223-b129 publication-title: J Biol Chem doi: 10.1074/jbc.R800011200 – volume: 284 start-page: 14245 year: 2009 ident: emboj2010223-b126 publication-title: J Biol Chem doi: 10.1074/jbc.M806902200 – volume: 364 start-page: 1169 year: 2004 ident: emboj2010223-b54 publication-title: Lancet doi: 10.1016/S0140-6736(04)17104-3 – volume: 26 start-page: 11915 year: 2006 ident: emboj2010223-b70 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.3821-06.2006 – volume: 441 start-page: 1157 year: 2006 ident: emboj2010223-b98 publication-title: Nature doi: 10.1038/nature04788 – ident: emboj2010223-b14 – ident: emboj2010223-b52 – volume: 271 start-page: 3180 year: 2004 ident: emboj2010223-b59 publication-title: Eur J Biochem doi: 10.1111/j.1432-1033.2004.04250.x – volume: 273 start-page: 9443 year: 1998 ident: emboj2010223-b21 publication-title: J Biol Chem doi: 10.1074/jbc.273.16.9443 – volume: 439 start-page: 125 year: 2008 ident: emboj2010223-b109 publication-title: Neurosci Lett doi: 10.1016/j.neulet.2008.05.005 – volume: 105 start-page: 19666 year: 2008 ident: emboj2010223-b57 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0807826105 – volume: 72 start-page: 175 year: 2003 ident: emboj2010223-b12 publication-title: Annu Rev Biochem doi: 10.1146/annurev.biochem.72.121801.161504 – volume: 37 start-page: 583 year: 2003 ident: emboj2010223-b108 publication-title: Neuron doi: 10.1016/S0896-6273(03)00024-2 – volume: 36 start-page: 315 year: 2007 ident: emboj2010223-b75 publication-title: Eur Biophys J doi: 10.1007/s00249-006-0097-z – volume: 45 start-page: 3386 year: 2006 ident: emboj2010223-b101 publication-title: Biochemistry doi: 10.1021/bi052344d – volume: 27 start-page: 12413 year: 2007 ident: emboj2010223-b31 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.0719-07.2007 – volume: 281 start-page: 37972 year: 2006 ident: emboj2010223-b30 publication-title: J Biol Chem doi: 10.1074/jbc.M606059200 – volume: 36 start-page: e38 year: 2008 ident: emboj2010223-b42 publication-title: Nucleic Acids Res doi: 10.1093/nar/gkn084 – volume: 1193 start-page: 219 year: 1994 ident: emboj2010223-b134 publication-title: Biochim Biophys Acta doi: 10.1016/0005-2736(94)90156-2 – volume: 21 start-page: 21966 year: 2004 ident: emboj2010223-b91 publication-title: J Biol Chem doi: 10.1074/jbc.M401076200 – volume: 419 start-page: 808 year: 2002 ident: emboj2010223-b51 publication-title: Nature doi: 10.1038/nature01135 – volume: 19 start-page: 3919 year: 1980b ident: emboj2010223-b107 publication-title: Biochemistry doi: 10.1021/bi00558a005 – volume: 304 start-page: 1158 year: 2004 ident: emboj2010223-b124 publication-title: Science doi: 10.1126/science.1096284 – volume: 92 start-page: 4012 year: 2007 ident: emboj2010223-b128 publication-title: Biophys J doi: 10.1529/biophysj.106.090043 – volume: 27 start-page: 1868 year: 2007 ident: emboj2010223-b49 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.5537-06.2007 – volume: 90 start-page: 2062 year: 2006 ident: emboj2010223-b10 publication-title: Biophys J doi: 10.1529/biophysj.105.071415 – volume: 8 start-page: 2804 year: 1988 ident: emboj2010223-b81 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.08-08-02804.1988 – volume: 278 start-page: 47199 year: 2003 ident: emboj2010223-b131 publication-title: J Biol Chem doi: 10.1074/jbc.M306769200 – volume: 65 start-page: 1272 year: 2008 ident: emboj2010223-b96 publication-title: Cell Mol Life Sci doi: 10.1007/s00018-008-7589-1 – volume: 8 start-page: 101 year: 2007 ident: emboj2010223-b44 publication-title: Nat Rev Mol Cell Biol doi: 10.1038/nrm2101 – volume: 106 start-page: 5645 year: 2009 ident: emboj2010223-b32 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0809232106 – volume: 279 start-page: 18614 year: 2004 ident: emboj2010223-b94 publication-title: J Biol Chem doi: 10.1074/jbc.M401135200 – volume: 103 start-page: 17 year: 2007 ident: emboj2010223-b123 publication-title: J Neurochem doi: 10.1111/j.1471-4159.2007.04764.x – volume: 24 start-page: 11165 year: 2004 ident: emboj2010223-b133 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.2559-04.2004 – volume: 1778 start-page: 1112 year: 2008 ident: emboj2010223-b36 publication-title: Biochim Biophys Acta doi: 10.1016/j.bbamem.2008.01.012 – volume: 685 start-page: 87 year: 1982 ident: emboj2010223-b34 publication-title: Biochim Biophys Acta doi: 10.1016/0005-2736(82)90038-4 – volume: 372 start-page: 421 year: 2007 ident: emboj2010223-b20 publication-title: Methods Mol Biol doi: 10.1007/978-1-59745-365-3_30 – volume: 170 start-page: 27 year: 1999 ident: emboj2010223-b95 publication-title: J Membr Biol doi: 10.1007/s002329900535 – volume: 28 start-page: 3256 year: 2009 ident: emboj2010223-b63 publication-title: EMBO J doi: 10.1038/emboj.2009.257 – volume: 3 start-page: e2455 year: 2008 ident: emboj2010223-b132 publication-title: PLoS One doi: 10.1371/journal.pone.0002455 – volume: 130 start-page: 7796 year: 2008b ident: emboj2010223-b29 publication-title: J Am Chem Soc doi: 10.1021/ja801594s – volume: 41 start-page: 2015 year: 2009 ident: emboj2010223-b97 publication-title: Int J Biochem Cell Biol doi: 10.1016/j.biocel.2009.05.008 – volume: 28 start-page: 12305 year: 2008 ident: emboj2010223-b86 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.3088-08.2008 – volume: 13 start-page: 453 year: 2003 ident: emboj2010223-b116 publication-title: Curr Opin Struct Biol doi: 10.1016/S0959-440X(03)00107-6 – volume: 302 start-page: 841 year: 2003 ident: emboj2010223-b111 publication-title: Science doi: 10.1126/science.1090278 – volume: 20 start-page: 4093 year: 1981 ident: emboj2010223-b114 publication-title: Biochemistry doi: 10.1021/bi00517a023 – volume: 14 start-page: 340 year: 2004 ident: emboj2010223-b46 publication-title: Curr Biol doi: 10.1016/j.cub.2004.02.004 – volume: 279 start-page: 6943 year: 2004 ident: emboj2010223-b39 publication-title: J Biol Chem doi: 10.1074/jbc.M309204200 – volume: 301 start-page: 891 year: 2003 ident: emboj2010223-b55 publication-title: Biochem Biophys Res Commun doi: 10.1016/S0006-291X(03)00050-0 – volume: 24 start-page: 3153 year: 2006 ident: emboj2010223-b71 publication-title: Eur J Neurosci doi: 10.1111/j.1460-9568.2006.05210.x – volume: 19 start-page: 3919 year: 1980a ident: emboj2010223-b106 publication-title: Biochemistry doi: 10.1021/bi00558a005 – volume: 101 start-page: 14966 year: 2004 ident: emboj2010223-b7 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0406283101 – reference: 16239241 - Hum Mol Genet. 2005 Dec 15;14(24):3801-11 – reference: 17652776 - Cell Biochem Biophys. 2007;47(2):285-99 – reference: 17039359 - Eur Biophys J. 2007 Apr;36(4-5):315-26 – reference: 17331951 - J Biol Chem. 2007 May 4;282(18):13680-91 – reference: 17110340 - Cell. 2006 Nov 17;127(4):831-46 – reference: 18261456 - Biochim Biophys Acta. 2008 Apr;1778(4):1112-9 – reference: 19546216 - J Biol Chem. 2009 Aug 21;284(34):22938-51 – reference: 18514418 - Neurosci Lett. 2008 Jul 11;439(2):125-8 – reference: 17573347 - J Biol Chem. 2007 Aug 24;282(34):24970-9 – reference: 16339880 - Biophys J. 2006 Mar 1;90(5):1661-75 – reference: 19066219 - Proc Natl Acad Sci U S A. 2008 Dec 16;105(50):19666-71 – reference: 9756856 - J Biol Chem. 1998 Oct 9;273(41):26292-4 – reference: 18440504 - Exp Cell Res. 2008 Jun 10;314(10):2076-89 – reference: 15265037 - Eur J Biochem. 2004 Aug;271(15):3180-9 – reference: 12351643 - J Biol Chem. 2002 Dec 13;277(50):48984-92 – reference: 18314714 - Methods Mol Biol. 2007;372:3-16 – reference: 14985362 - J Biol Chem. 2004 Apr 30;279(18):18614-22 – reference: 10707987 - Neuron. 2000 Jan;25(1):239-52 – reference: 17108165 - J Neurosci. 2006 Nov 15;26(46):11915-22 – reference: 9278044 - Nature. 1997 Aug 28;388(6645):839-40 – reference: 7857654 - Neuron. 1995 Feb;14(2):467-75 – reference: 12397350 - Nature. 2002 Oct 24;419(6909):808-14 – reference: 12815044 - J Biol Chem. 2003 Sep 26;278(39):37530-5 – reference: 16672981 - Nature. 2006 Jun 29;441(7097):1162-6 – reference: 15784737 - Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5215-20 – reference: 12972428 - J Biol Chem. 2003 Nov 21;278(47):47199-208 – reference: 15615727 - J Biol Chem. 2005 Mar 11;280(10):9595-603 – reference: 12589796 - Biochem Biophys Res Commun. 2003 Feb 21;301(4):891-8 – reference: 17623039 - J Neurochem. 2007 Oct;103(1):17-37 – reference: 18322646 - Cell Mol Life Sci. 2008 Apr;65(7-8):1272-84 – reference: 10398758 - J Membr Biol. 1999 Jul 1;170(1):27-38 – reference: 17156376 - Eur J Neurosci. 2006 Dec;24(11):3153-62 – reference: 18258594 - J Biol Chem. 2008 Apr 18;283(16):10992-1003 – reference: 16896109 - JAMA. 2006 Aug 9;296(6):661-70 – reference: 16855830 - Acta Neuropathol. 2006 Sep;112(3):261-5 – reference: 18314743 - Methods Mol Biol. 2007;372:421-30 – reference: 20049710 - EMBO Mol Med. 2009 May;1(2):99-111 – reference: 8770209 - Biophys J. 1996 Jan;70(1):330-8 – reference: 12597857 - Neuron. 2003 Feb 20;37(4):583-95 – reference: 19182805 - Nat Genet. 2009 Mar;41(3):308-15 – reference: 18245082 - J Biol Chem. 2008 Apr 4;283(14):9089-100 – reference: 7470445 - Biochemistry. 1980 Dec 23;19(26):6011-21 – reference: 16672980 - Nature. 2006 Jun 29;441(7097):1157-61 – reference: 14607841 - J Biol Chem. 2004 Feb 20;279(8):6943-51 – reference: 17314283 - J Neurosci. 2007 Feb 21;27(8):1868-78 – reference: 17369418 - Biophys J. 2007 Jun 1;92(11):4012-29 – reference: 17989306 - J Neurosci. 2007 Nov 7;27(45):12413-8 – reference: 14688212 - J Histochem Cytochem. 2004 Jan;52(1):1-12 – reference: 20152114 - Neuron. 2010 Jan 14;65(1):66-79 – reference: 15451225 - Lancet. 2004 Sep 25-Oct 1;364(9440):1169-71 – reference: 9529252 - Cell. 1998 Mar 20;92(6):759-72 – reference: 19481095 - J Mol Biol. 2009 Jul 24;390(4):775-90 – reference: 19020024 - J Neurosci. 2008 Nov 19;28(47):12305-17 – reference: 15891389 - Curr Opin Lipidol. 2005 Jun;16(3):287-94 – reference: 16166095 - J Biol Chem. 2005 Dec 30;280(52):43179-87 – reference: 15038157 - Biotechniques. 2004 Mar;36(3):418-22, 424 – reference: 20098416 - Nat Cell Biol. 2010 Feb;12(2):119-31 – reference: 15465911 - Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14966-71 – reference: 10619028 - Mol Cell. 1999 Nov;4(5):815-26 – reference: 16767175 - Genome. 2006 May;49(5):505-10 – reference: 19745811 - EMBO J. 2009 Oct 21;28(20):3256-68 – reference: 17885598 - Neuroreport. 2007 Oct 8;18(15):1543-6 – reference: 17287515 - J Neurosci. 2007 Feb 7;27(6):1405-10 – reference: 17882252 - Nat Rev Neurosci. 2007 Oct;8(10):743-54 – reference: 20577776 - Cell Mol Life Sci. 2010 Oct;67(20):3435-47 – reference: 18980610 - Traffic. 2009 Feb;10(2):218-34 – reference: 16361343 - Biophys J. 2006 Mar 15;90(6):2062-74 – reference: 16269331 - Cell. 2005 Nov 4;123(3):383-96 – reference: 15606901 - J Neurochem. 2005 Jan;92(1):114-22 – reference: 7059594 - Biochim Biophys Acta. 1982 Feb 8;685(1):87-93 – reference: 10934145 - Am J Pathol. 2000 Aug;157(2):401-10 – reference: 19088817 - Genome. 2008 Dec;51(12):1040-6 – reference: 10964942 - J Neurosci. 2000 Sep 1;20(17):6365-73 – reference: 16172208 - J Cell Biol. 2005 Sep 26;170(7):1067-78 – reference: 19915575 - Nat Genet. 2009 Dec;41(12):1308-12 – reference: 9560156 - Nature. 1998 Apr 9;392(6676):605-8 – reference: 17003040 - J Biol Chem. 2006 Dec 8;281(49):37972-9 – reference: 19126542 - J Biol Chem. 2009 Mar 13;284(11):7177-89 – reference: 16055544 - Biophys J. 2005 Oct;89(4):2458-72 – reference: 1935914 - EMBO J. 1991 Dec;10(12):3959-70 – reference: 11784292 - Eur J Biochem. 2002 Jan;269(1):2-12 – reference: 15536128 - Proc Natl Acad Sci U S A. 2004 Nov 23;101(47):16466-71 – reference: 16794039 - Science. 2006 Jul 21;313(5785):324-8 – reference: 19891973 - J Mol Biol. 2010 Jan 22;395(3):627-42 – reference: 15087508 - Science. 2004 May 21;304(5674):1158-60 – reference: 17928812 - Nat Rev Mol Cell Biol. 2007 Nov;8(11):870-9 – reference: 6893276 - Biochemistry. 1980 Aug 19;19(17):3919-23 – reference: 16399671 - J Neurosci. 2006 Jan 4;26(1):41-50 – reference: 19098006 - J Biol Chem. 2009 Feb 13;284(7):4230-7 – reference: 19293380 - Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5645-50 – reference: 16519533 - Biochemistry. 2006 Mar 14;45(10):3386-95 – reference: 14972687 - Curr Biol. 2004 Feb 17;14(4):340-5 – reference: 18512917 - J Am Chem Soc. 2008 Jun 25;130(25):7796-7 – reference: 17168787 - Curr Protein Pept Sci. 2006 Dec;7(6):539-52 – reference: 14550906 - Neurosci Lett. 2003 Nov 6;351(1):29-32 – reference: 9545270 - J Biol Chem. 1998 Apr 17;273(16):9443-9 – reference: 15028717 - J Biol Chem. 2004 May 21;279(21):21966-75 – reference: 15878861 - J Biol Chem. 2005 Jul 1;280(26):25060-70 – reference: 10777786 - J Neurosci. 2000 May 1;20(9):3214-20 – reference: 15196967 - Brain Res. 2004 Jul 2;1013(1):51-9 – reference: 20203200 - J Neurosci. 2010 Mar 3;30(9):3409-18 – reference: 14527322 - Annu Rev Biochem. 2003;72:175-207 – reference: 18162536 - Proc Natl Acad Sci U S A. 2008 Jan 8;105(1):145-50 – reference: 18560593 - PLoS One. 2008;3(6):e2455 – reference: 19220042 - Biochemistry. 2009 Mar 24;48(11):2304-6 – reference: 11733371 - Am J Pathol. 2001 Dec;159(6):2215-25 – reference: 11284690 - Biochemistry. 2001 Apr 10;40(14):4340-8 – reference: 12388586 - J Neurosci. 2002 Oct 15;22(20):8797-807 – reference: 19279012 - J Biol Chem. 2009 May 15;284(20):13843-55 – reference: 8054342 - Biochim Biophys Acta. 1994 Aug 3;1193(2):219-25 – reference: 18332041 - Nucleic Acids Res. 2008 Apr;36(7):e38 – reference: 14593171 - Science. 2003 Oct 31;302(5646):841 – reference: 13986422 - J Cell Biol. 1963 Apr;17:208-12 – reference: 10535963 - Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12571-6 – reference: 15181200 - Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):9103-8 – reference: 7563032 - J Membr Biol. 1995 Jul;146(1):1-14 – reference: 17245412 - Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12 – reference: 18821550 - Chembiochem. 2008 Oct 13;9(15):2411-6 – reference: 12944275 - Biophys J. 2003 Sep;85(3):1585-99 – reference: 19460457 - Int J Biochem Cell Biol. 2009 Oct;41(10):2015-24 – reference: 18372247 - J Biol Chem. 2008 May 16;283(20):13501-5 – reference: 7284312 - Biochemistry. 1981 Jul 7;20(14):4093-9 – reference: 15590933 - J Neurosci. 2004 Dec 8;24(49):11165-70 – reference: 19293155 - J Biol Chem. 2009 May 22;284(21):14245-57 – reference: 19915576 - Nat Genet. 2009 Dec;41(12):1303-7 – reference: 16455667 - J Biol Chem. 2006 Apr 7;281(14):9251-9 – reference: 14985429 - J Neurosci. 2004 Feb 25;24(8):1888-96 – reference: 14685248 - Nature. 2003 Dec 18;426(6968):884-90 – reference: 3411354 - J Neurosci. 1988 Aug;8(8):2804-15 – reference: 19492085 - PLoS One. 2009;4(5):e5701 – reference: 12948775 - Curr Opin Struct Biol. 2003 Aug;13(4):453-66 – reference: 16795004 - Mov Disord. 2006 Oct;21(10):1703-8 |
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| Snippet | Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The... Aggregation of α-synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The... Aggregation of alpha -synuclein ( alpha S) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders.... This study demonstrates that α-synuclein, which is implicated in the pathogenesis of Parkinson's disease, regulates mitochondrial dynamics by direct inhibition... |
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| SubjectTerms | alpha-Synuclein - genetics alpha-Synuclein - metabolism Animals Caenorhabditis elegans Caenorhabditis elegans - cytology Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Cell Line EMBO20 EMBO27 Humans Immunohistochemistry Intracellular Signaling Peptides and Proteins - genetics Intracellular Signaling Peptides and Proteins - metabolism Membrane Fusion - physiology mitochondria Mitochondria - metabolism Mitochondria - ultrastructure neurodegeneration Oncogene Proteins - genetics Oncogene Proteins - metabolism Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease Protein Deglycase DJ-1 Protein Kinases - genetics Protein Kinases - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism α-synuclein |
| Title | Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1 |
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