Structural basis of polyamine transport by human ATP13A2 (PARK9)
Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transpor...
Saved in:
Published in | Molecular cell Vol. 81; no. 22; pp. 4635 - 4649.e8 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
18.11.2021
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson's disease. To understand the polyamine transport mechanism of ATP13A2, we determined high-resolution cryoelectron microscopy (cryo-EM) structures of human ATP13A2 in five distinct conformational intermediates, which together, represent a near-complete transport cycle of ATP13A2. The structural basis of the polyamine specificity was revealed by an endogenous polyamine molecule bound to a narrow, elongated cavity within the transmembrane domain. The structures show an atypical transport path for a water-soluble substrate, in which polyamines may exit within the cytosolic leaflet of the membrane. Our study provides important mechanistic insights into polyamine transport and a framework to understand the functions and mechanisms of P5B-ATPases.
[Display omitted]
•High-resolution cryo-EM structures of human ATP13A2 in five distinct conformations•Unique features of ATP13A2 in comparison to other P-type ATPases•Structural basis of polyamine substrate binding to the membrane domain of ATP13A2•Conformational changes along the transport cycle and a model for polyamine transport
The P-type ATPase ATP13A2 is an endo-/lysosomal polyamine transporter, defects of which are implicated in hereditary forms of Parkinson disease. Sim et al. report structures of human ATP13A2 in five distinct conformations, representing a near-complete catalytic cycle. This work reveals the mechanistic basis of polyamine recognition and transport by ATP13A2. |
---|---|
AbstractList | Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson’s disease. To understand the polyamine transport mechanism of ATP13A2, we determined high-resolution cryo-EM structures of human ATP13A2 in five distinct conformational intermediates, which together represent a near-complete transport cycle of ATP13A2. The structural basis of the polyamine specificity was revealed by an endogenous polyamine molecule bound to a narrow, elongated cavity within the transmembrane domain. The structures show an atypical transport path for a water-soluble substrate, where polyamines may exit within the cytosolic leaflet of the membrane. Our study provides important mechanistic insights into polyamine transport and a framework to understand functions and mechanisms of P5B-ATPases.
The P-type ATPase ATP13A2 is an endo-/lysosomes polyamine transporter, defects of which are implicated in hereditary forms of Parkinson’s disease. Sim et al. report structures of human ATP13A2 in five distinct conformations, representing a near-complete catalytic cycle. This work reveals the mechanistic basis of polyamine recognition and transport by ATP13A2. Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson's disease. To understand the polyamine transport mechanism of ATP13A2, we determined high-resolution cryoelectron microscopy (cryo-EM) structures of human ATP13A2 in five distinct conformational intermediates, which together, represent a near-complete transport cycle of ATP13A2. The structural basis of the polyamine specificity was revealed by an endogenous polyamine molecule bound to a narrow, elongated cavity within the transmembrane domain. The structures show an atypical transport path for a water-soluble substrate, in which polyamines may exit within the cytosolic leaflet of the membrane. Our study provides important mechanistic insights into polyamine transport and a framework to understand the functions and mechanisms of P5B-ATPases. Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson's disease. To understand the polyamine transport mechanism of ATP13A2, we determined high-resolution cryoelectron microscopy (cryo-EM) structures of human ATP13A2 in five distinct conformational intermediates, which together, represent a near-complete transport cycle of ATP13A2. The structural basis of the polyamine specificity was revealed by an endogenous polyamine molecule bound to a narrow, elongated cavity within the transmembrane domain. The structures show an atypical transport path for a water-soluble substrate, in which polyamines may exit within the cytosolic leaflet of the membrane. Our study provides important mechanistic insights into polyamine transport and a framework to understand the functions and mechanisms of P5B-ATPases. [Display omitted] •High-resolution cryo-EM structures of human ATP13A2 in five distinct conformations•Unique features of ATP13A2 in comparison to other P-type ATPases•Structural basis of polyamine substrate binding to the membrane domain of ATP13A2•Conformational changes along the transport cycle and a model for polyamine transport The P-type ATPase ATP13A2 is an endo-/lysosomal polyamine transporter, defects of which are implicated in hereditary forms of Parkinson disease. Sim et al. report structures of human ATP13A2 in five distinct conformations, representing a near-complete catalytic cycle. This work reveals the mechanistic basis of polyamine recognition and transport by ATP13A2. |
Author | von Bülow, Sören Sim, Sue Im Hummer, Gerhard Park, Eunyong |
AuthorAffiliation | 5 Lead contact 2 Department of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany 3 Institute for Biophysics, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany 1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA 4 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA |
AuthorAffiliation_xml | – name: 1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA – name: 5 Lead contact – name: 2 Department of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany – name: 3 Institute for Biophysics, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany – name: 4 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA |
Author_xml | – sequence: 1 givenname: Sue Im orcidid: 0000-0003-3560-101X surname: Sim fullname: Sim, Sue Im organization: Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA – sequence: 2 givenname: Sören surname: von Bülow fullname: von Bülow, Sören organization: Department of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany – sequence: 3 givenname: Gerhard orcidid: 0000-0001-7768-746X surname: Hummer fullname: Hummer, Gerhard organization: Department of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany – sequence: 4 givenname: Eunyong orcidid: 0000-0003-2994-5174 surname: Park fullname: Park, Eunyong email: eunyong_park@berkeley.edu organization: Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34715013$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kElPwzAQhS0EYv8HCOUIhwYvSWxfEBViE0hUUM6W40zAVWIXO0HqvyfQsl04zUjz5s2bbwetO-8AoQOCU4JJcTJLW98YaFKKKUmxSDHha2ibYMlHGSmy9VVPeZFvoZ0YZxiTLBdyE22xjJMcE7aNzh670JuuD7pJSh1tTHydzH2z0K11kHRBuzj3oUvKRfLSt9ol4-mEsDFNjibjh1t5vIc2at1E2F_VXfR0eTE9vx7d3V_dnI_vRianshvJUggtdCnzrAbgAjNW8koXtNKa5hnjsipZJYgGgQGXhgswoCWtCIOaE8520enSd96XLVQG3JCtUfNgWx0Wymur_k6cfVHP_k2JAmec54PB0cog-NceYqdaGwd-jXbg-6hoLgcig5AN0mwpNcHHGKD-PkOw-oCvZmoJX33AV1go_Bnx8HfE76Uv2j8_wADqzUJQ0VhwBiobwHSq8vb_C-9YS5lA |
CitedBy_id | crossref_primary_10_1016_j_celrep_2022_111760 crossref_primary_10_1042_BST20221543 crossref_primary_10_1038_s41467_023_37815_z crossref_primary_10_3389_fneur_2023_1252400 crossref_primary_10_1016_j_jbc_2023_105352 crossref_primary_10_1146_annurev_biochem_071322_021330 crossref_primary_10_3390_biom13020337 crossref_primary_10_3390_biom13060918 crossref_primary_10_1016_j_bbamcr_2022_119354 crossref_primary_10_1016_j_sbi_2023_102531 crossref_primary_10_1002_mds_29759 crossref_primary_10_1080_15548627_2023_2214031 crossref_primary_10_1016_j_coisb_2021_100408 crossref_primary_10_1126_sciadv_add9742 crossref_primary_10_1038_s41467_023_42828_9 crossref_primary_10_1038_s41467_023_37741_0 crossref_primary_10_1002_bies_202200052 crossref_primary_10_1007_s44211_024_00626_3 |
Cites_doi | 10.1002/pro.5560051004 10.1073/pnas.1121406109 10.1016/j.softx.2015.06.001 10.1042/BJ20120739 10.1016/j.celrep.2020.108208 10.1093/nar/gkh381 10.1126/science.aay3353 10.1146/annurev.biophys.093008.131331 10.1074/jbc.RA120.013908 10.1371/journal.pone.0193228 10.1063/1.328693 10.1002/pro.3235 10.1073/pnas.1112368109 10.1107/S0907444909042073 10.25080/Majora-629e541a-00e 10.1074/jbc.271.21.12205 10.1371/journal.pone.0146021 10.1371/journal.pcbi.1002708 10.1038/nature02981 10.1042/bj3250289 10.1021/ct300646g 10.1002/ajmg.b.31214 10.1093/brain/aww307 10.1038/ejhg.2016.42 10.1212/01.wnl.0000260963.08711.08 10.1038/ng1884 10.1021/acs.jctc.5b00209 10.1016/j.bbabio.2010.04.010 10.1038/s41592-019-0580-y 10.1212/01.wnl.0000310427.72236.68 10.1038/srep06836 10.1016/j.jsb.2005.07.007 10.1073/pnas.1508220112 10.1016/j.neuron.2018.07.027 10.1021/ac9509519 10.1038/nmeth.4169 10.1038/nrm2330 10.1042/BCJ20200249 10.1016/j.celrep.2020.108363 10.1038/s41586-020-1968-7 10.1016/j.sbi.2010.06.007 10.1186/s40246-019-0203-9 10.1093/hmg/dds089 10.1002/mdc3.12353 10.1038/emboj.2012.170 10.1371/journal.pone.0039942 10.1155/2014/371256 10.1016/j.celrep.2020.108101 10.3389/fchem.2018.00010 10.1002/mgg3.1052 10.1038/ng.300 10.1038/nrm1354 10.1002/iub.230 10.1523/JNEUROSCI.5575-11.2012 10.1038/nature11900 10.1186/s12896-017-0400-3 10.1063/1.448118 10.3389/fphys.2017.00371 10.1038/nature07939 10.1126/science.1099366 10.1083/jcb.201804165 10.1038/nature06419 10.1038/35015017 10.1107/S2059798318006551 10.1016/j.biocel.2009.07.009 10.1016/S1044-0305(98)00157-3 10.1038/s41589-020-0529-6 10.1073/pnas.1922342117 10.1007/s10048-010-0259-0 10.1016/j.tins.2019.10.002 10.1002/mds.22728 10.1002/humu.21527 10.1063/1.2408420 10.1016/j.neurobiolaging.2011.12.035 10.1038/s41586-019-1344-7 10.1016/j.braindev.2018.05.017 10.1016/j.ympev.2007.10.023 10.1080/13554794.2019.1625928 10.1074/jbc.M503071200 10.1107/S0907444910007493 10.1042/BST20190124 10.1016/0006-2952(86)90024-9 10.7554/eLife.62163 10.1038/nature06418 10.1002/jcc.20084 10.1096/fj.09-135889 10.1073/pnas.181342398 10.1042/bj3440633 10.1126/science.abc5809 10.1021/ct3009655 |
ContentType | Journal Article |
Copyright | 2021 Elsevier Inc. Copyright © 2021 Elsevier Inc. All rights reserved. |
Copyright_xml | – notice: 2021 Elsevier Inc. – notice: Copyright © 2021 Elsevier Inc. All rights reserved. |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM |
DOI | 10.1016/j.molcel.2021.08.017 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1097-4164 |
EndPage | 4649.e8 |
ExternalDocumentID | 10_1016_j_molcel_2021_08_017 34715013 S1097276521006845 |
Genre | Research Support, U.S. Gov't, Non-P.H.S Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: T32 GM008295 |
GroupedDBID | --- --K -DZ -~X 0R~ 123 1~5 2WC 4.4 457 4G. 5RE 62- 7-5 AACTN AAEDW AAFTH AAIAV AAKRW AAKUH AALRI AAUCE AAVLU AAXUO ABJNI ABMAC ABMWF ABVKL ACGFO ACGFS ACNCT ADBBV ADEZE ADJPV AEFWE AENEX AEXQZ AFFNX AFTJW AGKMS AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ ASPBG AVWKF AZFZN BAWUL CS3 DIK DU5 E3Z EBS F5P FCP FDB FEDTE FIRID HH5 HVGLF IH2 IHE IXB J1W JIG KQ8 L7B M3Z M41 N9A NCXOZ O-L O9- OK1 P2P RCE ROL RPZ SDG SES SSZ TR2 WQ6 ZA5 0SF AAEDT AAHBH AAMRU ADVLN AKAPO AKRWK CGR CUY CVF ECM EIF NPM RIG .55 .GJ 29M 3O- 53G 5VS 6I. AAIKJ AAQFI AAQXK AAYXX ADMUD AGHFR CITATION EJD FGOYB HZ~ OZT R2- UHS X7M ZGI ZXP 7X8 5PM |
ID | FETCH-LOGICAL-c529t-9b88a8ab954fee78033b7da62daa254379db3d81ae80e0bc78ecea92d13ef7173 |
IEDL.DBID | ABVKL |
ISSN | 1097-2765 |
IngestDate | Tue Sep 17 21:35:10 EDT 2024 Fri Aug 16 20:59:19 EDT 2024 Thu Sep 26 17:40:22 EDT 2024 Sat Sep 28 08:24:30 EDT 2024 Fri Feb 23 02:38:56 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 22 |
Keywords | polyamine P5B-ATPase Parkinson's disease transporter spermine membrane protein P-type ATPase lysosome cryo-EM |
Language | English |
License | Copyright © 2021 Elsevier Inc. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c529t-9b88a8ab954fee78033b7da62daa254379db3d81ae80e0bc78ecea92d13ef7173 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 E.P. conceived and supervised the project. S.I.S. prepared cryo-EM samples and performed biochemical assays. E.P. and S.I.S. collected and analyzed cryo-EM data, built atomic models, interpreted results. S.v.B. and G.H. performed MD simulations and interpreted results. E.P. and S.I.S. wrote the manuscript with input from all authors. All authors edited the manuscript. Author contributions |
ORCID | 0000-0003-2994-5174 0000-0003-3560-101X 0000-0001-7768-746X |
OpenAccessLink | http://www.cell.com/article/S1097276521006845/pdf |
PMID | 34715013 |
PQID | 2590137533 |
PQPubID | 23479 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_8604775 proquest_miscellaneous_2590137533 crossref_primary_10_1016_j_molcel_2021_08_017 pubmed_primary_34715013 elsevier_sciencedirect_doi_10_1016_j_molcel_2021_08_017 |
PublicationCentury | 2000 |
PublicationDate | 2021-11-18 |
PublicationDateYYYYMMDD | 2021-11-18 |
PublicationDate_xml | – month: 11 year: 2021 text: 2021-11-18 day: 18 |
PublicationDecade | 2020 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Molecular cell |
PublicationTitleAlternate | Mol Cell |
PublicationYear | 2021 |
Publisher | Elsevier Inc |
Publisher_xml | – name: Elsevier Inc |
References | Sørensen, Holemans, van Veen, Martin, Arslan, Haagendahl, Holen, Hamouda, Eggermont, Palmgren, Vangheluwe (bib69) 2018; 13 Heinick, Urban, Roth, Spies, Nunes, Phanstiel, Liebau, Lüersen (bib34) 2010; 24 Palmgren, Nissen (bib54) 2011; 40 Yung, Green (bib90) 1986; 35 Bai, You, Jain, Duan, Kovach, Graham, Li (bib5) 2020; 9 Dolinsky, Nielsen, McCammon, Baker (bib20) 2004; 32 Mastronarde (bib46) 2005; 152 Park, Mehta, Cooper, Veivers, Heimbach, Stiller, Kubisch, Fung, Krainc, Mackay-Sim, Sue (bib55) 2011; 32 Pegg (bib57) 2009; 61 Punjani, Rubinstein, Fleet, Brubaker (bib60) 2017; 14 Gowers, Linke, Barnoud, Reddy, Melo, Seyler, Dotson, Domanski, Buchoux, Kenney (bib30) 2016 Bublitz, Poulsen, Morth, Nissen (bib9) 2010; 20 Feng, Zhao, Li, Nie, Yang, Wang, Wu, Liao, Zou (bib26) 2020; 32 Igarashi, Kashiwagi (bib39) 2010; 42 McKenna, Sim, Ordureau, Wei, Harper, Shao, Park (bib47) 2020; 369 Djarmati, Hagenah, Reetz, Winkler, Behrens, Pawlack, Lohmann, Ramirez, Tadić, Brüggemann (bib19) 2009; 24 Hiasa, Miyaji, Haruna, Takeuchi, Harada, Moriyama, Yamamoto, Omote, Moriyama (bib35) 2014; 30 Afonine, Poon, Read, Sobolev, Terwilliger, Urzhumtsev, Adams (bib3) 2018; 74 Parrinello, Rahman (bib56) 1981; 52 Toyoshima, Nakasako, Nomura, Ogawa (bib75) 2000; 405 Chovancova, Pavelka, Benes, Strnad, Brezovsky, Kozlikova, Gora, Sustr, Klvana, Medek (bib13) 2012; 8 Hamouda, Van den Haute, Vanhoutte, Sannerud, Azfar, Mayer, Cortes Calabuig, Swinnen, Agostinis, Baekelandt (bib32) 2021; 296 Dyla, Basse Hansen, Nissen, Kjaergaard (bib21) 2019; 47 de Jong, Singh, Bennett, Arnarez, Wassenaar, Schäfer, Periole, Tieleman, Marrink (bib15) 2013; 9 Lorent, Levental, Ganesan, Rivera-Longsworth, Sezgin, Doktorova, Lyman, Levental (bib45) 2020; 16 Morth, Pedersen, Toustrup-Jensen, Sørensen, Petersen, Andersen, Vilsen, Nissen (bib50) 2007; 450 Sugiyama, Matsuo, Maenaka, Vassylyev, Matsushima, Kashiwagi, Igarashi, Morikawa (bib71) 1996; 5 Emsley, Lohkamp, Scott, Cowtan (bib22) 2010; 66 Scholz, Suppmann (bib65) 2017; 17 Abbas, Govindappa, Sheerin, Bhatia, Muthane (bib1) 2016; 4 Kühlbrandt (bib42) 2004; 5 Kashiwagi, Pistocchi, Shibuya, Sugiyama, Morikawa, Igarashi (bib41) 1996; 271 Nakanishi, Nishizawa, Segawa, Nureki, Fujiyoshi, Nagata, Abe (bib51) 2020; 32 Toyoshima, Nomura, Tsuda (bib76) 2004; 432 Suleiman, Hamwi, El-Hattab (bib72) 2018; 40 Igarashi, Kashiwagi (bib38) 1999; 344 Ning, Kanai, Tomiyama, Li, Funayama, Yoshino, Sato, Asahina, Kuwabara, Takeda (bib52) 2008; 70 De La Hera, Corradi, Adamo, De Tezanos Pinto (bib16) 2013; 450 McNeil-Gauthier, Brais, Rouleau, Anoja, Ducharme (bib48) 2019; 25 Tegunov, Cramer (bib73) 2019; 16 Estiar, Leveille, Spiegelman, Dupre, Trempe, Rouleau, Gan-Or (bib23) 2020; 8 Fujita, Fujita, Iuchi, Yamada, Kobayashi, Urano, Kobayashi, Yamaguchi-Shinozaki, Shinozaki (bib27) 2012; 109 Pettersen, Goddard, Huang, Couch, Greenblatt, Meng, Ferrin (bib58) 2004; 25 Spataro, Kousi, Farhan, Willer, Ross, Dion, Rouleau, Daly, Neale, La Bella, Katsanis (bib70) 2019; 13 van Meer, Voelker, Feigenson (bib80) 2008; 9 Ritz, Baty, Streibig, Gerhard (bib63) 2015; 10 Grunewald, Arns, Seibler, Rakovic, Munchau, Ramirez, Sue, Klein (bib31) 2012; 33 Møller, Asp, Holm, Palmgren (bib49) 2008; 46 van Veen, Martin, Van den Haute, Benoy, Lyons, Vanhoutte, Kahler, Decuypere, Gelders, Lambie (bib81) 2020; 578 Wilm, Mann (bib87) 1996; 68 Hiraizumi, Yamashita, Nishizawa, Nureki (bib36) 2019; 365 Shinoda, Ogawa, Cornelius, Toyoshima (bib66) 2009; 459 Goddard, Huang, Meng, Pettersen, Couch, Morris, Ferrin (bib29) 2018; 27 Twomey, Yelshanskaya, Vassilevski, Sobolevsky (bib77) 2018; 99 Ramirez, Heimbach, Gründemann, Stiller, Hampshire, Cid, Goebel, Mubaidin, Wriekat, Roeper (bib62) 2006; 38 Aouida, Leduc, Poulin, Ramotar (bib4) 2005; 280 Bussi, Donadio, Parrinello (bib10) 2007; 126 López, Sovova, van Eerden, de Vries, Marrink (bib43) 2013; 9 Qin, Zhao, Zou, Shen, Wang (bib61) 2020; 33 Wassenaar, Ingólfsson, Böckmann, Tieleman, Marrink (bib85) 2015; 11 Usenovic, Tresse, Mazzulli, Taylor, Krainc (bib78) 2012; 32 Dehay, Ramirez, Martinez-Vicente, Perier, Canron, Doudnikoff, Vital, Vila, Klein, Bezard (bib17) 2012; 109 Wallings, Humble, Ward, Wade-Martins (bib83) 2019; 42 Yang, Xu (bib89) 2014; 2014 Bras, Verloes, Schneider, Mole, Guerreiro (bib8) 2012; 21 Chen, Arendall, Headd, Keedy, Immormino, Kapral, Murray, Richardson, Richardson (bib11) 2010; 66 Gitler, Chesi, Geddie, Strathearn, Hamamichi, Hill, Caldwell, Caldwell, Cooper, Rochet, Lindquist (bib28) 2009; 41 Holemans, Sørensen, van Veen, Martin, Hermans, Kemmer, Van den Haute, Baekelandt, Günther Pomorski, Agostinis (bib37) 2015; 112 Olesen, Picard, Winther, Gyrup, Morth, Oxvig, Møller, Nissen (bib53) 2007; 450 Podhajska, Musso, Trancikova, Stafa, Moser, Sonnay, Glauser, Moore (bib59) 2012; 7 Clausen, Hilbers, Poulsen (bib14) 2017; 8 Sørensen, Buch-Pedersen, Palmgren (bib68) 2010; 1797 Timcenko, Lyons, Januliene, Ulstrup, Dieudonné, Montigny, Ash, Karlsen, Boesen, Kühlbrandt (bib74) 2019; 571 Estrada-Cuzcano, Martin, Chamova, Synofzik, Timmann, Holemans, Andreeva, Reichbauer, De Rycke, Chang (bib24) 2017; 140 van de Warrenburg, Schouten, de Bot, Vermeer, Meijer, Pennings, Gilissen, Willemsen, Scheffer, Kamsteeg (bib79) 2016; 24 Handa, Fatima, Mattoo (bib33) 2018; 6 Williams (bib86) 1997; 325 Abraham, Murtola, Schulz, Páll, Smith, Hess, Lindahl (bib2) 2015; 1-2 Juraschek, Dülcks, Karas (bib40) 1999; 10 López-Marqués, Gourdon, Günther Pomorski, Palmgren (bib44) 2020; 477 Vrijsen, Besora-Casals, van Veen, Zielich, Van den Haute, Hamouda, Fischer, Ghesquière, Tournev, Agostinis (bib82) 2020; 117 Winther, Bublitz, Karlsen, Møller, Hansen, Nissen, Buch-Pedersen (bib88) 2013; 495 Chen, Lin, Juan, Hu, Hsiao, Chang, Chao, Chen, Lee, Wang (bib12) 2011; 156B Wang, Tan, Chen, Han, Tian, Tan, Wu, Cui, Chen, Li (bib84) 2019; 218 Di Fonzo, Chien, Socal, Giraudo, Tassorelli, Iliceto, Fabbrini, Marconi, Fincati, Abbruzzese (bib18) 2007; 68 Santoro, Breedveld, Manganelli, Iodice, Pisciotta, Nolano, Punzo, Quarantelli, Pappatà, Di Fonzo (bib64) 2011; 12 Baker, Sept, Joseph, Holst, McCammon (bib6) 2001; 98 Berendsen, Postma, van Gunsteren, DiNola, Haak (bib7) 1984; 81 Sørensen, Møller, Nissen (bib67) 2004; 304 Exner, Lutz, Haass, Winklhofer (bib25) 2012; 31 Ramirez (10.1016/j.molcel.2021.08.017_bib62) 2006; 38 Dehay (10.1016/j.molcel.2021.08.017_bib17) 2012; 109 van de Warrenburg (10.1016/j.molcel.2021.08.017_bib79) 2016; 24 Sørensen (10.1016/j.molcel.2021.08.017_bib69) 2018; 13 Wang (10.1016/j.molcel.2021.08.017_bib84) 2019; 218 Usenovic (10.1016/j.molcel.2021.08.017_bib78) 2012; 32 Chen (10.1016/j.molcel.2021.08.017_bib11) 2010; 66 Holemans (10.1016/j.molcel.2021.08.017_bib37) 2015; 112 Igarashi (10.1016/j.molcel.2021.08.017_bib38) 1999; 344 Sørensen (10.1016/j.molcel.2021.08.017_bib68) 2010; 1797 McKenna (10.1016/j.molcel.2021.08.017_bib47) 2020; 369 Yung (10.1016/j.molcel.2021.08.017_bib90) 1986; 35 Dolinsky (10.1016/j.molcel.2021.08.017_bib20) 2004; 32 Kashiwagi (10.1016/j.molcel.2021.08.017_bib41) 1996; 271 López (10.1016/j.molcel.2021.08.017_bib43) 2013; 9 Wassenaar (10.1016/j.molcel.2021.08.017_bib85) 2015; 11 Winther (10.1016/j.molcel.2021.08.017_bib88) 2013; 495 Toyoshima (10.1016/j.molcel.2021.08.017_bib76) 2004; 432 Fujita (10.1016/j.molcel.2021.08.017_bib27) 2012; 109 Palmgren (10.1016/j.molcel.2021.08.017_bib54) 2011; 40 Scholz (10.1016/j.molcel.2021.08.017_bib65) 2017; 17 Estrada-Cuzcano (10.1016/j.molcel.2021.08.017_bib24) 2017; 140 Bai (10.1016/j.molcel.2021.08.017_bib5) 2020; 9 Nakanishi (10.1016/j.molcel.2021.08.017_bib51) 2020; 32 Gitler (10.1016/j.molcel.2021.08.017_bib28) 2009; 41 Baker (10.1016/j.molcel.2021.08.017_bib6) 2001; 98 Williams (10.1016/j.molcel.2021.08.017_bib86) 1997; 325 Grunewald (10.1016/j.molcel.2021.08.017_bib31) 2012; 33 Gowers (10.1016/j.molcel.2021.08.017_bib30) 2016 McNeil-Gauthier (10.1016/j.molcel.2021.08.017_bib48) 2019; 25 Sørensen (10.1016/j.molcel.2021.08.017_bib67) 2004; 304 Park (10.1016/j.molcel.2021.08.017_bib55) 2011; 32 Sugiyama (10.1016/j.molcel.2021.08.017_bib71) 1996; 5 Hiasa (10.1016/j.molcel.2021.08.017_bib35) 2014; 30 Suleiman (10.1016/j.molcel.2021.08.017_bib72) 2018; 40 Heinick (10.1016/j.molcel.2021.08.017_bib34) 2010; 24 Juraschek (10.1016/j.molcel.2021.08.017_bib40) 1999; 10 Punjani (10.1016/j.molcel.2021.08.017_bib60) 2017; 14 Feng (10.1016/j.molcel.2021.08.017_bib26) 2020; 32 van Veen (10.1016/j.molcel.2021.08.017_bib81) 2020; 578 Di Fonzo (10.1016/j.molcel.2021.08.017_bib18) 2007; 68 Abbas (10.1016/j.molcel.2021.08.017_bib1) 2016; 4 Ritz (10.1016/j.molcel.2021.08.017_bib63) 2015; 10 Santoro (10.1016/j.molcel.2021.08.017_bib64) 2011; 12 Abraham (10.1016/j.molcel.2021.08.017_bib2) 2015; 1-2 Mastronarde (10.1016/j.molcel.2021.08.017_bib46) 2005; 152 Bras (10.1016/j.molcel.2021.08.017_bib8) 2012; 21 de Jong (10.1016/j.molcel.2021.08.017_bib15) 2013; 9 Hiraizumi (10.1016/j.molcel.2021.08.017_bib36) 2019; 365 Chen (10.1016/j.molcel.2021.08.017_bib12) 2011; 156B Møller (10.1016/j.molcel.2021.08.017_bib49) 2008; 46 Toyoshima (10.1016/j.molcel.2021.08.017_bib75) 2000; 405 Pegg (10.1016/j.molcel.2021.08.017_bib57) 2009; 61 Wallings (10.1016/j.molcel.2021.08.017_bib83) 2019; 42 Clausen (10.1016/j.molcel.2021.08.017_bib14) 2017; 8 Estiar (10.1016/j.molcel.2021.08.017_bib23) 2020; 8 Handa (10.1016/j.molcel.2021.08.017_bib33) 2018; 6 Vrijsen (10.1016/j.molcel.2021.08.017_bib82) 2020; 117 Spataro (10.1016/j.molcel.2021.08.017_bib70) 2019; 13 Podhajska (10.1016/j.molcel.2021.08.017_bib59) 2012; 7 Parrinello (10.1016/j.molcel.2021.08.017_bib56) 1981; 52 Ning (10.1016/j.molcel.2021.08.017_bib52) 2008; 70 Emsley (10.1016/j.molcel.2021.08.017_bib22) 2010; 66 Bussi (10.1016/j.molcel.2021.08.017_bib10) 2007; 126 Kühlbrandt (10.1016/j.molcel.2021.08.017_bib42) 2004; 5 Tegunov (10.1016/j.molcel.2021.08.017_bib73) 2019; 16 Yang (10.1016/j.molcel.2021.08.017_bib89) 2014; 2014 Lorent (10.1016/j.molcel.2021.08.017_bib45) 2020; 16 Chovancova (10.1016/j.molcel.2021.08.017_bib13) 2012; 8 Bublitz (10.1016/j.molcel.2021.08.017_bib9) 2010; 20 Goddard (10.1016/j.molcel.2021.08.017_bib29) 2018; 27 Qin (10.1016/j.molcel.2021.08.017_bib61) 2020; 33 Timcenko (10.1016/j.molcel.2021.08.017_bib74) 2019; 571 Dyla (10.1016/j.molcel.2021.08.017_bib21) 2019; 47 Shinoda (10.1016/j.molcel.2021.08.017_bib66) 2009; 459 Exner (10.1016/j.molcel.2021.08.017_bib25) 2012; 31 López-Marqués (10.1016/j.molcel.2021.08.017_bib44) 2020; 477 Twomey (10.1016/j.molcel.2021.08.017_bib77) 2018; 99 Djarmati (10.1016/j.molcel.2021.08.017_bib19) 2009; 24 Pettersen (10.1016/j.molcel.2021.08.017_bib58) 2004; 25 Aouida (10.1016/j.molcel.2021.08.017_bib4) 2005; 280 Afonine (10.1016/j.molcel.2021.08.017_bib3) 2018; 74 Berendsen (10.1016/j.molcel.2021.08.017_bib7) 1984; 81 Igarashi (10.1016/j.molcel.2021.08.017_bib39) 2010; 42 Wilm (10.1016/j.molcel.2021.08.017_bib87) 1996; 68 De La Hera (10.1016/j.molcel.2021.08.017_bib16) 2013; 450 Morth (10.1016/j.molcel.2021.08.017_bib50) 2007; 450 Olesen (10.1016/j.molcel.2021.08.017_bib53) 2007; 450 Hamouda (10.1016/j.molcel.2021.08.017_bib32) 2021; 296 van Meer (10.1016/j.molcel.2021.08.017_bib80) 2008; 9 |
References_xml | – volume: 70 start-page: 1491 year: 2008 end-page: 1493 ident: bib52 article-title: PARK9-linked parkinsonism in eastern Asia: mutation detection in ATP13A2 and clinical phenotype publication-title: Neurology contributor: fullname: Takeda – volume: 81 start-page: 3684 year: 1984 end-page: 3690 ident: bib7 article-title: Molecular dynamics with coupling to an external bath publication-title: J. Chem. Phys. contributor: fullname: Haak – volume: 24 start-page: 2104 year: 2009 end-page: 2111 ident: bib19 article-title: ATP13A2 variants in early-onset Parkinson’s disease patients and controls publication-title: Mov. Disord. contributor: fullname: Brüggemann – volume: 13 start-page: 19 year: 2019 ident: bib70 article-title: Mutations in ATP13A2 (PARK9) are associated with an amyotrophic lateral sclerosis-like phenotype, implicating this locus in further phenotypic expansion publication-title: Hum. Genomics contributor: fullname: Katsanis – volume: 46 start-page: 619 year: 2008 end-page: 634 ident: bib49 article-title: Phylogenetic analysis of P5 P-type ATPases, a eukaryotic lineage of secretory pathway pumps publication-title: Mol. Phylogenet. Evol. contributor: fullname: Palmgren – volume: 14 start-page: 290 year: 2017 end-page: 296 ident: bib60 article-title: cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination publication-title: Nat. Methods contributor: fullname: Brubaker – volume: 25 start-page: 133 year: 2019 end-page: 137 ident: bib48 article-title: Successful treatment of psychosis in a patient with Kufor-Rakeb syndrome with low dose aripiprazole: a case report publication-title: Neurocase contributor: fullname: Ducharme – volume: 450 start-page: 47 year: 2013 end-page: 53 ident: bib16 article-title: Parkinson’s disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake publication-title: Biochem. J. contributor: fullname: De Tezanos Pinto – volume: 33 start-page: 108363 year: 2020 ident: bib61 article-title: An endoplasmic reticulum ATPase safeguards endoplasmic reticulum identity by removing ectopically localized mitochondrial proteins publication-title: Cell Rep. contributor: fullname: Wang – volume: 1-2 start-page: 19 year: 2015 end-page: 25 ident: bib2 article-title: GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers publication-title: SoftwareX contributor: fullname: Lindahl – volume: 98 start-page: 10037 year: 2001 end-page: 10041 ident: bib6 article-title: Electrostatics of nanosystems: application to microtubules and the ribosome publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: McCammon – volume: 6 start-page: 10 year: 2018 ident: bib33 article-title: Polyamines: bio-molecules with diverse functions in plant and human health and disease publication-title: Front Chem. contributor: fullname: Mattoo – volume: 9 start-page: 112 year: 2008 end-page: 124 ident: bib80 article-title: Membrane lipids: where they are and how they behave publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Feigenson – volume: 156B start-page: 720 year: 2011 end-page: 729 ident: bib12 article-title: ATP13A2 variability in Taiwanese Parkinson’s disease publication-title: Am. J. Med. Genet. B. Neuropsychiatr. Genet. contributor: fullname: Wang – volume: 450 start-page: 1036 year: 2007 end-page: 1042 ident: bib53 article-title: The structural basis of calcium transport by the calcium pump publication-title: Nature contributor: fullname: Nissen – volume: 61 start-page: 880 year: 2009 end-page: 894 ident: bib57 article-title: Mammalian polyamine metabolism and function publication-title: IUBMB Life contributor: fullname: Pegg – volume: 2014 start-page: 371256 year: 2014 ident: bib89 article-title: Mutations in the ATP13A2 gene and Parkinsonism: a preliminary review publication-title: BioMed Res. Int. contributor: fullname: Xu – volume: 32 start-page: 108101 year: 2020 ident: bib26 article-title: CATP-8/P5A ATPase regulates ER processing of the DMA-1 receptor for dendritic branching publication-title: Cell Rep. contributor: fullname: Zou – volume: 344 start-page: 633 year: 1999 end-page: 642 ident: bib38 article-title: Polyamine transport in bacteria and yeast publication-title: Biochem. J. contributor: fullname: Kashiwagi – volume: 68 start-page: 1557 year: 2007 end-page: 1562 ident: bib18 article-title: ATP13A2 missense mutations in juvenile parkinsonism and young onset Parkinson disease publication-title: Neurology contributor: fullname: Abbruzzese – volume: 5 start-page: 1984 year: 1996 end-page: 1990 ident: bib71 article-title: The 1.8-A X-ray structure of the publication-title: Protein Sci. contributor: fullname: Morikawa – volume: 109 start-page: 9611 year: 2012 end-page: 9616 ident: bib17 article-title: Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Bezard – volume: 52 start-page: 7182 year: 1981 end-page: 7190 ident: bib56 article-title: Polymorphic transitions in single crystals: a new molecular dynamics method publication-title: J. Appl. Phys. contributor: fullname: Rahman – volume: 9 start-page: 687 year: 2013 end-page: 697 ident: bib15 article-title: Improved parameters for the martini coarse-grained protein force field publication-title: J. Chem. Theory Comput. contributor: fullname: Marrink – volume: 7 start-page: e39942 year: 2012 ident: bib59 article-title: Common pathogenic effects of missense mutations in the P-type ATPase ATP13A2 (PARK9) associated with early-onset parkinsonism publication-title: PLoS ONE contributor: fullname: Moore – volume: 24 start-page: 206 year: 2010 end-page: 217 ident: bib34 article-title: Caenorhabditis elegans P5B-type ATPase CATP-5 operates in polyamine transport and is crucial for norspermidine-mediated suppression of RNA interference publication-title: FASEB J. contributor: fullname: Lüersen – volume: 369 start-page: eabc5809 year: 2020 ident: bib47 article-title: The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase publication-title: Science contributor: fullname: Park – volume: 30 start-page: 6836 year: 2014 ident: bib35 article-title: Identification of a mammalian vesicular polyamine transporter publication-title: Sci. Rep. contributor: fullname: Moriyama – volume: 40 start-page: 243 year: 2011 end-page: 266 ident: bib54 article-title: P-type ATPases publication-title: Annu. Rev. Biophys. contributor: fullname: Nissen – volume: 5 start-page: 282 year: 2004 end-page: 295 ident: bib42 article-title: Biology, structure and mechanism of P-type ATPases publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Kühlbrandt – volume: 27 start-page: 14 year: 2018 end-page: 25 ident: bib29 article-title: UCSF ChimeraX: Meeting modern challenges in visualization and analysis publication-title: Protein Sci. contributor: fullname: Ferrin – volume: 477 start-page: 3769 year: 2020 end-page: 3790 ident: bib44 article-title: The transport mechanism of P4 ATPase lipid flippases publication-title: Biochem. J. contributor: fullname: Palmgren – volume: 38 start-page: 1184 year: 2006 end-page: 1191 ident: bib62 article-title: Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase publication-title: Nat. Genet. contributor: fullname: Roeper – volume: 32 start-page: 108208 year: 2020 ident: bib51 article-title: Transport cycle of plasma membrane flippase ATP11C by cryo-EM publication-title: Cell Rep. contributor: fullname: Abe – volume: 74 start-page: 531 year: 2018 end-page: 544 ident: bib3 article-title: Real-space refinement in PHENIX for cryo-EM and crystallography publication-title: Acta Crystallogr. D Struct. Biol. contributor: fullname: Adams – volume: 66 start-page: 12 year: 2010 end-page: 21 ident: bib11 article-title: MolProbity: all-atom structure validation for macromolecular crystallography publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Richardson – volume: 66 start-page: 486 year: 2010 end-page: 501 ident: bib22 article-title: Features and development of Coot publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Cowtan – volume: 126 start-page: 014101 year: 2007 ident: bib10 article-title: Canonical sampling through velocity rescaling publication-title: J. Chem. Phys. contributor: fullname: Parrinello – volume: 41 start-page: 308 year: 2009 end-page: 315 ident: bib28 article-title: α-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity publication-title: Nat. Genet. contributor: fullname: Lindquist – volume: 450 start-page: 1043 year: 2007 end-page: 1049 ident: bib50 article-title: Crystal structure of the sodium-potassium pump publication-title: Nature contributor: fullname: Nissen – volume: 12 start-page: 33 year: 2011 end-page: 39 ident: bib64 article-title: Novel ATP13A2 (PARK9) homozygous mutation in a family with marked phenotype variability publication-title: Neurogenetics contributor: fullname: Di Fonzo – volume: 17 start-page: 83 year: 2017 ident: bib65 article-title: A new single-step protocol for rapid baculovirus-driven protein production in insect cells publication-title: BMC Biotechnol. contributor: fullname: Suppmann – volume: 16 start-page: 1146 year: 2019 end-page: 1152 ident: bib73 article-title: Real-time cryo-electron microscopy data preprocessing with Warp publication-title: Nat. Methods contributor: fullname: Cramer – volume: 218 start-page: 267 year: 2019 end-page: 284 ident: bib84 article-title: ATP13A2 facilitates HDAC6 recruitment to lysosome to promote autophagosome-lysosome fusion publication-title: J. Cell Biol. contributor: fullname: Li – volume: 24 start-page: 1460 year: 2016 end-page: 1466 ident: bib79 article-title: Clinical exome sequencing for cerebellar ataxia and spastic paraplegia uncovers novel gene-disease associations and unanticipated rare disorders publication-title: Eur. J. Hum. Genet. contributor: fullname: Kamsteeg – volume: 13 start-page: e0193228 year: 2018 ident: bib69 article-title: Parkinson disease related ATP13A2 evolved early in animal evolution publication-title: PLoS One contributor: fullname: Vangheluwe – volume: 42 start-page: 899 year: 2019 end-page: 912 ident: bib83 article-title: Lysosomal dysfunction at the centre of Parkinson’s disease and frontotemporal dementia/amyotrophic lateral sclerosis publication-title: Trends Neurosci. contributor: fullname: Wade-Martins – volume: 495 start-page: 265 year: 2013 end-page: 269 ident: bib88 article-title: The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm publication-title: Nature contributor: fullname: Buch-Pedersen – volume: 20 start-page: 431 year: 2010 end-page: 439 ident: bib9 article-title: In and out of the cation pumps: P-type ATPase structure revisited publication-title: Curr. Opin. Struct. Biol. contributor: fullname: Nissen – volume: 432 start-page: 361 year: 2004 end-page: 368 ident: bib76 article-title: Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues publication-title: Nature contributor: fullname: Tsuda – volume: 304 start-page: 1672 year: 2004 end-page: 1675 ident: bib67 article-title: Phosphoryl transfer and calcium ion occlusion in the calcium pump publication-title: Science contributor: fullname: Nissen – volume: 117 start-page: 31198 year: 2020 end-page: 31207 ident: bib82 article-title: ATP13A2-mediated endo-lysosomal polyamine export counters mitochondrial oxidative stress publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Agostinis – volume: 8 start-page: e1002708 year: 2012 ident: bib13 article-title: CAVER 3.0: a tool for the analysis of transport pathways in dynamic protein structures publication-title: PLoS Comput. Biol. contributor: fullname: Medek – volume: 578 start-page: 419 year: 2020 end-page: 424 ident: bib81 article-title: ATP13A2 deficiency disrupts lysosomal polyamine export publication-title: Nature contributor: fullname: Lambie – volume: 32 start-page: 956 year: 2011 end-page: 964 ident: bib55 article-title: Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism publication-title: Hum. Mutat. contributor: fullname: Sue – volume: 16 start-page: 644 year: 2020 end-page: 652 ident: bib45 article-title: Plasma membranes are asymmetric in lipid unsaturation, packing and protein shape publication-title: Nat. Chem. Biol. contributor: fullname: Levental – volume: 152 start-page: 36 year: 2005 end-page: 51 ident: bib46 article-title: Automated electron microscope tomography using robust prediction of specimen movements publication-title: J. Struct. Biol. contributor: fullname: Mastronarde – volume: 140 start-page: 287 year: 2017 end-page: 305 ident: bib24 article-title: Loss-of-function mutations in the publication-title: Brain contributor: fullname: Chang – volume: 459 start-page: 446 year: 2009 end-page: 450 ident: bib66 article-title: Crystal structure of the sodium-potassium pump at 2.4 A resolution publication-title: Nature contributor: fullname: Toyoshima – volume: 10 start-page: e0146021 year: 2015 ident: bib63 article-title: Dose-response analysis using R publication-title: PLoS One contributor: fullname: Gerhard – volume: 33 start-page: 1843.e1 year: 2012 end-page: 1843.e7 ident: bib31 article-title: ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome publication-title: Neurobiol. Aging contributor: fullname: Klein – volume: 112 start-page: 9040 year: 2015 end-page: 9045 ident: bib37 article-title: A lipid switch unlocks Parkinson’s disease-associated ATP13A2 publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Agostinis – volume: 9 start-page: 1694 year: 2013 end-page: 1708 ident: bib43 article-title: Martini force field parameters for glycolipids publication-title: J. Chem. Theory Comput. contributor: fullname: Marrink – volume: 21 start-page: 2646 year: 2012 end-page: 2650 ident: bib8 article-title: Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis publication-title: Hum. Mol. Genet. contributor: fullname: Guerreiro – volume: 1797 start-page: 846 year: 2010 end-page: 855 ident: bib68 article-title: Structural divergence between the two subgroups of P5 ATPases publication-title: Biochim. Biophys. Acta contributor: fullname: Palmgren – volume: 271 start-page: 12205 year: 1996 end-page: 12208 ident: bib41 article-title: Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD protein publication-title: J. Biol. Chem. contributor: fullname: Igarashi – volume: 405 start-page: 647 year: 2000 end-page: 655 ident: bib75 article-title: Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution publication-title: Nature contributor: fullname: Ogawa – volume: 365 start-page: 1149 year: 2019 end-page: 1155 ident: bib36 article-title: Cryo-EM structures capture the transport cycle of the P4-ATPase flippase publication-title: Science contributor: fullname: Nureki – volume: 325 start-page: 289 year: 1997 end-page: 297 ident: bib86 article-title: Interactions of polyamines with ion channels publication-title: Biochem. J. contributor: fullname: Williams – start-page: 98 year: 2016 end-page: 105 ident: bib30 article-title: MDAnalysis: a Python package for the rapid analysis of molecular dynamics simulations publication-title: Proceedings of the 15th Python in Science Conference: SciPy contributor: fullname: Kenney – volume: 40 start-page: 824 year: 2018 end-page: 826 ident: bib72 article-title: ATP13A2 novel mutations causing a rare form of juvenile-onset Parkinson disease publication-title: Brain Dev. contributor: fullname: El-Hattab – volume: 31 start-page: 3038 year: 2012 end-page: 3062 ident: bib25 article-title: Mitochondrial dysfunction in Parkinson’s disease: molecular mechanisms and pathophysiological consequences publication-title: EMBO J. contributor: fullname: Winklhofer – volume: 571 start-page: 366 year: 2019 end-page: 370 ident: bib74 article-title: Structure and autoregulation of a P4-ATPase lipid flippase publication-title: Nature contributor: fullname: Kühlbrandt – volume: 10 start-page: 300 year: 1999 end-page: 308 ident: bib40 article-title: Nanoelectrospray--more than just a minimized-flow electrospray ionization source publication-title: J. Am. Soc. Mass Spectrom. contributor: fullname: Karas – volume: 25 start-page: 1605 year: 2004 end-page: 1612 ident: bib58 article-title: UCSF chimera—a visualization system for exploratory research and analysis publication-title: J. Comput. Chem. contributor: fullname: Ferrin – volume: 32 start-page: 4240 year: 2012 end-page: 4246 ident: bib78 article-title: Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity publication-title: J. Neurosci. contributor: fullname: Krainc – volume: 280 start-page: 24267 year: 2005 end-page: 24276 ident: bib4 article-title: AGP2 encodes the major permease for high affinity polyamine import in publication-title: J. Biol. Chem. contributor: fullname: Ramotar – volume: 4 start-page: 132 year: 2016 end-page: 135 ident: bib1 article-title: Exome sequencing identifies a novel homozygous missense publication-title: Mov. Disord. Clin. Pract. (Hoboken) contributor: fullname: Muthane – volume: 47 start-page: 1247 year: 2019 end-page: 1257 ident: bib21 article-title: Structural dynamics of P-type ATPase ion pumps publication-title: Biochem. Soc. Trans. contributor: fullname: Kjaergaard – volume: 8 start-page: 371 year: 2017 ident: bib14 article-title: The structure and function of the Na,K-ATPase isoforms in health and disease publication-title: Front. Physiol. contributor: fullname: Poulsen – volume: 11 start-page: 2144 year: 2015 end-page: 2155 ident: bib85 article-title: Computational lipidomics with insane: a versatile tool for generating custom membranes for molecular simulations publication-title: J. Chem. Theory Comput. contributor: fullname: Marrink – volume: 35 start-page: 4037 year: 1986 end-page: 4041 ident: bib90 article-title: The binding of polyamines to phospholipid bilayers publication-title: Biochem. Pharmacol. contributor: fullname: Green – volume: 296 start-page: 100182 year: 2021 ident: bib32 article-title: ATP13A3 is a major component of the enigmatic mammalian polyamine transport system publication-title: J. Biol. Chem. contributor: fullname: Baekelandt – volume: 8 start-page: e1052 year: 2020 ident: bib23 article-title: Clinical and genetic analysis of ATP13A2 in hereditary spastic paraplegia expands the phenotype publication-title: Mol. Genet. Genomic Med. contributor: fullname: Gan-Or – volume: 99 start-page: 956 year: 2018 end-page: 968.e4 ident: bib77 article-title: Mechanisms of channel block in calcium-permeable AMPA receptors publication-title: Neuron contributor: fullname: Sobolevsky – volume: 68 start-page: 1 year: 1996 end-page: 8 ident: bib87 article-title: Analytical properties of the nanoelectrospray ion source publication-title: Anal. Chem. contributor: fullname: Mann – volume: 9 start-page: e62163 year: 2020 ident: bib5 article-title: Transport mechanism of P4 ATPase phosphatidylcholine flippases publication-title: eLife contributor: fullname: Li – volume: 42 start-page: 39 year: 2010 end-page: 51 ident: bib39 article-title: Modulation of cellular function by polyamines publication-title: Int. J. Biochem. Cell Biol. contributor: fullname: Kashiwagi – volume: 32 year: 2004 ident: bib20 article-title: PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations publication-title: Nucleic Acids Res. contributor: fullname: Baker – volume: 109 start-page: 6343 year: 2012 end-page: 6347 ident: bib27 article-title: Natural variation in a polyamine transporter determines paraquat tolerance in Arabidopsis publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Shinozaki – volume: 5 start-page: 1984 year: 1996 ident: 10.1016/j.molcel.2021.08.017_bib71 article-title: The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding publication-title: Protein Sci. doi: 10.1002/pro.5560051004 contributor: fullname: Sugiyama – volume: 109 start-page: 6343 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib27 article-title: Natural variation in a polyamine transporter determines paraquat tolerance in Arabidopsis publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1121406109 contributor: fullname: Fujita – volume: 1-2 start-page: 19 year: 2015 ident: 10.1016/j.molcel.2021.08.017_bib2 article-title: GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers publication-title: SoftwareX doi: 10.1016/j.softx.2015.06.001 contributor: fullname: Abraham – volume: 450 start-page: 47 year: 2013 ident: 10.1016/j.molcel.2021.08.017_bib16 article-title: Parkinson’s disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake publication-title: Biochem. J. doi: 10.1042/BJ20120739 contributor: fullname: De La Hera – volume: 32 start-page: 108208 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib51 article-title: Transport cycle of plasma membrane flippase ATP11C by cryo-EM publication-title: Cell Rep. doi: 10.1016/j.celrep.2020.108208 contributor: fullname: Nakanishi – volume: 32 year: 2004 ident: 10.1016/j.molcel.2021.08.017_bib20 article-title: PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh381 contributor: fullname: Dolinsky – volume: 365 start-page: 1149 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib36 article-title: Cryo-EM structures capture the transport cycle of the P4-ATPase flippase publication-title: Science doi: 10.1126/science.aay3353 contributor: fullname: Hiraizumi – volume: 40 start-page: 243 year: 2011 ident: 10.1016/j.molcel.2021.08.017_bib54 article-title: P-type ATPases publication-title: Annu. Rev. Biophys. doi: 10.1146/annurev.biophys.093008.131331 contributor: fullname: Palmgren – volume: 296 start-page: 100182 year: 2021 ident: 10.1016/j.molcel.2021.08.017_bib32 article-title: ATP13A3 is a major component of the enigmatic mammalian polyamine transport system publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA120.013908 contributor: fullname: Hamouda – volume: 13 start-page: e0193228 year: 2018 ident: 10.1016/j.molcel.2021.08.017_bib69 article-title: Parkinson disease related ATP13A2 evolved early in animal evolution publication-title: PLoS One doi: 10.1371/journal.pone.0193228 contributor: fullname: Sørensen – volume: 52 start-page: 7182 year: 1981 ident: 10.1016/j.molcel.2021.08.017_bib56 article-title: Polymorphic transitions in single crystals: a new molecular dynamics method publication-title: J. Appl. Phys. doi: 10.1063/1.328693 contributor: fullname: Parrinello – volume: 27 start-page: 14 year: 2018 ident: 10.1016/j.molcel.2021.08.017_bib29 article-title: UCSF ChimeraX: Meeting modern challenges in visualization and analysis publication-title: Protein Sci. doi: 10.1002/pro.3235 contributor: fullname: Goddard – volume: 109 start-page: 9611 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib17 article-title: Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1112368109 contributor: fullname: Dehay – volume: 66 start-page: 12 year: 2010 ident: 10.1016/j.molcel.2021.08.017_bib11 article-title: MolProbity: all-atom structure validation for macromolecular crystallography publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444909042073 contributor: fullname: Chen – start-page: 98 year: 2016 ident: 10.1016/j.molcel.2021.08.017_bib30 article-title: MDAnalysis: a Python package for the rapid analysis of molecular dynamics simulations doi: 10.25080/Majora-629e541a-00e contributor: fullname: Gowers – volume: 271 start-page: 12205 year: 1996 ident: 10.1016/j.molcel.2021.08.017_bib41 article-title: Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD protein publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.21.12205 contributor: fullname: Kashiwagi – volume: 10 start-page: e0146021 year: 2015 ident: 10.1016/j.molcel.2021.08.017_bib63 article-title: Dose-response analysis using R publication-title: PLoS One doi: 10.1371/journal.pone.0146021 contributor: fullname: Ritz – volume: 8 start-page: e1002708 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib13 article-title: CAVER 3.0: a tool for the analysis of transport pathways in dynamic protein structures publication-title: PLoS Comput. Biol. doi: 10.1371/journal.pcbi.1002708 contributor: fullname: Chovancova – volume: 432 start-page: 361 year: 2004 ident: 10.1016/j.molcel.2021.08.017_bib76 article-title: Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues publication-title: Nature doi: 10.1038/nature02981 contributor: fullname: Toyoshima – volume: 325 start-page: 289 year: 1997 ident: 10.1016/j.molcel.2021.08.017_bib86 article-title: Interactions of polyamines with ion channels publication-title: Biochem. J. doi: 10.1042/bj3250289 contributor: fullname: Williams – volume: 9 start-page: 687 year: 2013 ident: 10.1016/j.molcel.2021.08.017_bib15 article-title: Improved parameters for the martini coarse-grained protein force field publication-title: J. Chem. Theory Comput. doi: 10.1021/ct300646g contributor: fullname: de Jong – volume: 156B start-page: 720 year: 2011 ident: 10.1016/j.molcel.2021.08.017_bib12 article-title: ATP13A2 variability in Taiwanese Parkinson’s disease publication-title: Am. J. Med. Genet. B. Neuropsychiatr. Genet. doi: 10.1002/ajmg.b.31214 contributor: fullname: Chen – volume: 140 start-page: 287 year: 2017 ident: 10.1016/j.molcel.2021.08.017_bib24 article-title: Loss-of-function mutations in the ATP13A2/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78) publication-title: Brain doi: 10.1093/brain/aww307 contributor: fullname: Estrada-Cuzcano – volume: 24 start-page: 1460 year: 2016 ident: 10.1016/j.molcel.2021.08.017_bib79 article-title: Clinical exome sequencing for cerebellar ataxia and spastic paraplegia uncovers novel gene-disease associations and unanticipated rare disorders publication-title: Eur. J. Hum. Genet. doi: 10.1038/ejhg.2016.42 contributor: fullname: van de Warrenburg – volume: 68 start-page: 1557 year: 2007 ident: 10.1016/j.molcel.2021.08.017_bib18 article-title: ATP13A2 missense mutations in juvenile parkinsonism and young onset Parkinson disease publication-title: Neurology doi: 10.1212/01.wnl.0000260963.08711.08 contributor: fullname: Di Fonzo – volume: 38 start-page: 1184 year: 2006 ident: 10.1016/j.molcel.2021.08.017_bib62 article-title: Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase publication-title: Nat. Genet. doi: 10.1038/ng1884 contributor: fullname: Ramirez – volume: 11 start-page: 2144 year: 2015 ident: 10.1016/j.molcel.2021.08.017_bib85 article-title: Computational lipidomics with insane: a versatile tool for generating custom membranes for molecular simulations publication-title: J. Chem. Theory Comput. doi: 10.1021/acs.jctc.5b00209 contributor: fullname: Wassenaar – volume: 1797 start-page: 846 year: 2010 ident: 10.1016/j.molcel.2021.08.017_bib68 article-title: Structural divergence between the two subgroups of P5 ATPases publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2010.04.010 contributor: fullname: Sørensen – volume: 16 start-page: 1146 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib73 article-title: Real-time cryo-electron microscopy data preprocessing with Warp publication-title: Nat. Methods doi: 10.1038/s41592-019-0580-y contributor: fullname: Tegunov – volume: 70 start-page: 1491 year: 2008 ident: 10.1016/j.molcel.2021.08.017_bib52 article-title: PARK9-linked parkinsonism in eastern Asia: mutation detection in ATP13A2 and clinical phenotype publication-title: Neurology doi: 10.1212/01.wnl.0000310427.72236.68 contributor: fullname: Ning – volume: 30 start-page: 6836 year: 2014 ident: 10.1016/j.molcel.2021.08.017_bib35 article-title: Identification of a mammalian vesicular polyamine transporter publication-title: Sci. Rep. doi: 10.1038/srep06836 contributor: fullname: Hiasa – volume: 152 start-page: 36 year: 2005 ident: 10.1016/j.molcel.2021.08.017_bib46 article-title: Automated electron microscope tomography using robust prediction of specimen movements publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.07.007 contributor: fullname: Mastronarde – volume: 112 start-page: 9040 year: 2015 ident: 10.1016/j.molcel.2021.08.017_bib37 article-title: A lipid switch unlocks Parkinson’s disease-associated ATP13A2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1508220112 contributor: fullname: Holemans – volume: 99 start-page: 956 year: 2018 ident: 10.1016/j.molcel.2021.08.017_bib77 article-title: Mechanisms of channel block in calcium-permeable AMPA receptors publication-title: Neuron doi: 10.1016/j.neuron.2018.07.027 contributor: fullname: Twomey – volume: 68 start-page: 1 year: 1996 ident: 10.1016/j.molcel.2021.08.017_bib87 article-title: Analytical properties of the nanoelectrospray ion source publication-title: Anal. Chem. doi: 10.1021/ac9509519 contributor: fullname: Wilm – volume: 14 start-page: 290 year: 2017 ident: 10.1016/j.molcel.2021.08.017_bib60 article-title: cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination publication-title: Nat. Methods doi: 10.1038/nmeth.4169 contributor: fullname: Punjani – volume: 9 start-page: 112 year: 2008 ident: 10.1016/j.molcel.2021.08.017_bib80 article-title: Membrane lipids: where they are and how they behave publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2330 contributor: fullname: van Meer – volume: 477 start-page: 3769 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib44 article-title: The transport mechanism of P4 ATPase lipid flippases publication-title: Biochem. J. doi: 10.1042/BCJ20200249 contributor: fullname: López-Marqués – volume: 33 start-page: 108363 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib61 article-title: An endoplasmic reticulum ATPase safeguards endoplasmic reticulum identity by removing ectopically localized mitochondrial proteins publication-title: Cell Rep. doi: 10.1016/j.celrep.2020.108363 contributor: fullname: Qin – volume: 578 start-page: 419 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib81 article-title: ATP13A2 deficiency disrupts lysosomal polyamine export publication-title: Nature doi: 10.1038/s41586-020-1968-7 contributor: fullname: van Veen – volume: 20 start-page: 431 year: 2010 ident: 10.1016/j.molcel.2021.08.017_bib9 article-title: In and out of the cation pumps: P-type ATPase structure revisited publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2010.06.007 contributor: fullname: Bublitz – volume: 13 start-page: 19 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib70 article-title: Mutations in ATP13A2 (PARK9) are associated with an amyotrophic lateral sclerosis-like phenotype, implicating this locus in further phenotypic expansion publication-title: Hum. Genomics doi: 10.1186/s40246-019-0203-9 contributor: fullname: Spataro – volume: 21 start-page: 2646 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib8 article-title: Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/dds089 contributor: fullname: Bras – volume: 4 start-page: 132 year: 2016 ident: 10.1016/j.molcel.2021.08.017_bib1 article-title: Exome sequencing identifies a novel homozygous missense ATP13A2 mutation publication-title: Mov. Disord. Clin. Pract. (Hoboken) doi: 10.1002/mdc3.12353 contributor: fullname: Abbas – volume: 31 start-page: 3038 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib25 article-title: Mitochondrial dysfunction in Parkinson’s disease: molecular mechanisms and pathophysiological consequences publication-title: EMBO J. doi: 10.1038/emboj.2012.170 contributor: fullname: Exner – volume: 7 start-page: e39942 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib59 article-title: Common pathogenic effects of missense mutations in the P-type ATPase ATP13A2 (PARK9) associated with early-onset parkinsonism publication-title: PLoS ONE doi: 10.1371/journal.pone.0039942 contributor: fullname: Podhajska – volume: 2014 start-page: 371256 year: 2014 ident: 10.1016/j.molcel.2021.08.017_bib89 article-title: Mutations in the ATP13A2 gene and Parkinsonism: a preliminary review publication-title: BioMed Res. Int. doi: 10.1155/2014/371256 contributor: fullname: Yang – volume: 32 start-page: 108101 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib26 article-title: CATP-8/P5A ATPase regulates ER processing of the DMA-1 receptor for dendritic branching publication-title: Cell Rep. doi: 10.1016/j.celrep.2020.108101 contributor: fullname: Feng – volume: 6 start-page: 10 year: 2018 ident: 10.1016/j.molcel.2021.08.017_bib33 article-title: Polyamines: bio-molecules with diverse functions in plant and human health and disease publication-title: Front Chem. doi: 10.3389/fchem.2018.00010 contributor: fullname: Handa – volume: 8 start-page: e1052 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib23 article-title: Clinical and genetic analysis of ATP13A2 in hereditary spastic paraplegia expands the phenotype publication-title: Mol. Genet. Genomic Med. doi: 10.1002/mgg3.1052 contributor: fullname: Estiar – volume: 41 start-page: 308 year: 2009 ident: 10.1016/j.molcel.2021.08.017_bib28 article-title: α-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity publication-title: Nat. Genet. doi: 10.1038/ng.300 contributor: fullname: Gitler – volume: 5 start-page: 282 year: 2004 ident: 10.1016/j.molcel.2021.08.017_bib42 article-title: Biology, structure and mechanism of P-type ATPases publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm1354 contributor: fullname: Kühlbrandt – volume: 61 start-page: 880 year: 2009 ident: 10.1016/j.molcel.2021.08.017_bib57 article-title: Mammalian polyamine metabolism and function publication-title: IUBMB Life doi: 10.1002/iub.230 contributor: fullname: Pegg – volume: 32 start-page: 4240 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib78 article-title: Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.5575-11.2012 contributor: fullname: Usenovic – volume: 495 start-page: 265 year: 2013 ident: 10.1016/j.molcel.2021.08.017_bib88 article-title: The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm publication-title: Nature doi: 10.1038/nature11900 contributor: fullname: Winther – volume: 17 start-page: 83 year: 2017 ident: 10.1016/j.molcel.2021.08.017_bib65 article-title: A new single-step protocol for rapid baculovirus-driven protein production in insect cells publication-title: BMC Biotechnol. doi: 10.1186/s12896-017-0400-3 contributor: fullname: Scholz – volume: 81 start-page: 3684 year: 1984 ident: 10.1016/j.molcel.2021.08.017_bib7 article-title: Molecular dynamics with coupling to an external bath publication-title: J. Chem. Phys. doi: 10.1063/1.448118 contributor: fullname: Berendsen – volume: 8 start-page: 371 year: 2017 ident: 10.1016/j.molcel.2021.08.017_bib14 article-title: The structure and function of the Na,K-ATPase isoforms in health and disease publication-title: Front. Physiol. doi: 10.3389/fphys.2017.00371 contributor: fullname: Clausen – volume: 459 start-page: 446 year: 2009 ident: 10.1016/j.molcel.2021.08.017_bib66 article-title: Crystal structure of the sodium-potassium pump at 2.4 A resolution publication-title: Nature doi: 10.1038/nature07939 contributor: fullname: Shinoda – volume: 304 start-page: 1672 year: 2004 ident: 10.1016/j.molcel.2021.08.017_bib67 article-title: Phosphoryl transfer and calcium ion occlusion in the calcium pump publication-title: Science doi: 10.1126/science.1099366 contributor: fullname: Sørensen – volume: 218 start-page: 267 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib84 article-title: ATP13A2 facilitates HDAC6 recruitment to lysosome to promote autophagosome-lysosome fusion publication-title: J. Cell Biol. doi: 10.1083/jcb.201804165 contributor: fullname: Wang – volume: 450 start-page: 1043 year: 2007 ident: 10.1016/j.molcel.2021.08.017_bib50 article-title: Crystal structure of the sodium-potassium pump publication-title: Nature doi: 10.1038/nature06419 contributor: fullname: Morth – volume: 405 start-page: 647 year: 2000 ident: 10.1016/j.molcel.2021.08.017_bib75 article-title: Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution publication-title: Nature doi: 10.1038/35015017 contributor: fullname: Toyoshima – volume: 74 start-page: 531 year: 2018 ident: 10.1016/j.molcel.2021.08.017_bib3 article-title: Real-space refinement in PHENIX for cryo-EM and crystallography publication-title: Acta Crystallogr. D Struct. Biol. doi: 10.1107/S2059798318006551 contributor: fullname: Afonine – volume: 42 start-page: 39 year: 2010 ident: 10.1016/j.molcel.2021.08.017_bib39 article-title: Modulation of cellular function by polyamines publication-title: Int. J. Biochem. Cell Biol. doi: 10.1016/j.biocel.2009.07.009 contributor: fullname: Igarashi – volume: 10 start-page: 300 year: 1999 ident: 10.1016/j.molcel.2021.08.017_bib40 article-title: Nanoelectrospray--more than just a minimized-flow electrospray ionization source publication-title: J. Am. Soc. Mass Spectrom. doi: 10.1016/S1044-0305(98)00157-3 contributor: fullname: Juraschek – volume: 16 start-page: 644 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib45 article-title: Plasma membranes are asymmetric in lipid unsaturation, packing and protein shape publication-title: Nat. Chem. Biol. doi: 10.1038/s41589-020-0529-6 contributor: fullname: Lorent – volume: 117 start-page: 31198 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib82 article-title: ATP13A2-mediated endo-lysosomal polyamine export counters mitochondrial oxidative stress publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1922342117 contributor: fullname: Vrijsen – volume: 12 start-page: 33 year: 2011 ident: 10.1016/j.molcel.2021.08.017_bib64 article-title: Novel ATP13A2 (PARK9) homozygous mutation in a family with marked phenotype variability publication-title: Neurogenetics doi: 10.1007/s10048-010-0259-0 contributor: fullname: Santoro – volume: 42 start-page: 899 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib83 article-title: Lysosomal dysfunction at the centre of Parkinson’s disease and frontotemporal dementia/amyotrophic lateral sclerosis publication-title: Trends Neurosci. doi: 10.1016/j.tins.2019.10.002 contributor: fullname: Wallings – volume: 24 start-page: 2104 year: 2009 ident: 10.1016/j.molcel.2021.08.017_bib19 article-title: ATP13A2 variants in early-onset Parkinson’s disease patients and controls publication-title: Mov. Disord. doi: 10.1002/mds.22728 contributor: fullname: Djarmati – volume: 32 start-page: 956 year: 2011 ident: 10.1016/j.molcel.2021.08.017_bib55 article-title: Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism publication-title: Hum. Mutat. doi: 10.1002/humu.21527 contributor: fullname: Park – volume: 126 start-page: 014101 year: 2007 ident: 10.1016/j.molcel.2021.08.017_bib10 article-title: Canonical sampling through velocity rescaling publication-title: J. Chem. Phys. doi: 10.1063/1.2408420 contributor: fullname: Bussi – volume: 33 start-page: 1843.e1 year: 2012 ident: 10.1016/j.molcel.2021.08.017_bib31 article-title: ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome publication-title: Neurobiol. Aging doi: 10.1016/j.neurobiolaging.2011.12.035 contributor: fullname: Grunewald – volume: 571 start-page: 366 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib74 article-title: Structure and autoregulation of a P4-ATPase lipid flippase publication-title: Nature doi: 10.1038/s41586-019-1344-7 contributor: fullname: Timcenko – volume: 40 start-page: 824 year: 2018 ident: 10.1016/j.molcel.2021.08.017_bib72 article-title: ATP13A2 novel mutations causing a rare form of juvenile-onset Parkinson disease publication-title: Brain Dev. doi: 10.1016/j.braindev.2018.05.017 contributor: fullname: Suleiman – volume: 46 start-page: 619 year: 2008 ident: 10.1016/j.molcel.2021.08.017_bib49 article-title: Phylogenetic analysis of P5 P-type ATPases, a eukaryotic lineage of secretory pathway pumps publication-title: Mol. Phylogenet. Evol. doi: 10.1016/j.ympev.2007.10.023 contributor: fullname: Møller – volume: 25 start-page: 133 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib48 article-title: Successful treatment of psychosis in a patient with Kufor-Rakeb syndrome with low dose aripiprazole: a case report publication-title: Neurocase doi: 10.1080/13554794.2019.1625928 contributor: fullname: McNeil-Gauthier – volume: 280 start-page: 24267 year: 2005 ident: 10.1016/j.molcel.2021.08.017_bib4 article-title: AGP2 encodes the major permease for high affinity polyamine import in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M503071200 contributor: fullname: Aouida – volume: 66 start-page: 486 year: 2010 ident: 10.1016/j.molcel.2021.08.017_bib22 article-title: Features and development of Coot publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444910007493 contributor: fullname: Emsley – volume: 47 start-page: 1247 year: 2019 ident: 10.1016/j.molcel.2021.08.017_bib21 article-title: Structural dynamics of P-type ATPase ion pumps publication-title: Biochem. Soc. Trans. doi: 10.1042/BST20190124 contributor: fullname: Dyla – volume: 35 start-page: 4037 year: 1986 ident: 10.1016/j.molcel.2021.08.017_bib90 article-title: The binding of polyamines to phospholipid bilayers publication-title: Biochem. Pharmacol. doi: 10.1016/0006-2952(86)90024-9 contributor: fullname: Yung – volume: 9 start-page: e62163 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib5 article-title: Transport mechanism of P4 ATPase phosphatidylcholine flippases publication-title: eLife doi: 10.7554/eLife.62163 contributor: fullname: Bai – volume: 450 start-page: 1036 year: 2007 ident: 10.1016/j.molcel.2021.08.017_bib53 article-title: The structural basis of calcium transport by the calcium pump publication-title: Nature doi: 10.1038/nature06418 contributor: fullname: Olesen – volume: 25 start-page: 1605 year: 2004 ident: 10.1016/j.molcel.2021.08.017_bib58 article-title: UCSF chimera—a visualization system for exploratory research and analysis publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 contributor: fullname: Pettersen – volume: 24 start-page: 206 year: 2010 ident: 10.1016/j.molcel.2021.08.017_bib34 article-title: Caenorhabditis elegans P5B-type ATPase CATP-5 operates in polyamine transport and is crucial for norspermidine-mediated suppression of RNA interference publication-title: FASEB J. doi: 10.1096/fj.09-135889 contributor: fullname: Heinick – volume: 98 start-page: 10037 year: 2001 ident: 10.1016/j.molcel.2021.08.017_bib6 article-title: Electrostatics of nanosystems: application to microtubules and the ribosome publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.181342398 contributor: fullname: Baker – volume: 344 start-page: 633 year: 1999 ident: 10.1016/j.molcel.2021.08.017_bib38 article-title: Polyamine transport in bacteria and yeast publication-title: Biochem. J. doi: 10.1042/bj3440633 contributor: fullname: Igarashi – volume: 369 start-page: eabc5809 year: 2020 ident: 10.1016/j.molcel.2021.08.017_bib47 article-title: The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase publication-title: Science doi: 10.1126/science.abc5809 contributor: fullname: McKenna – volume: 9 start-page: 1694 year: 2013 ident: 10.1016/j.molcel.2021.08.017_bib43 article-title: Martini force field parameters for glycolipids publication-title: J. Chem. Theory Comput. doi: 10.1021/ct3009655 contributor: fullname: López |
SSID | ssj0014589 |
Score | 2.5361524 |
Snippet | Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is... |
SourceID | pubmedcentral proquest crossref pubmed elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 4635 |
SubjectTerms | Animals Biological Transport Catalysis cryo-EM Cryoelectron Microscopy Cytosol - metabolism Humans Lipids - chemistry lysosome Lysosomes - chemistry membrane protein Molecular Dynamics Simulation P-type ATPase P5B-ATPase Parkinson Disease - metabolism Parkinson's disease Phosphorylation polyamine Polyamines - chemistry Protein Conformation Protein Domains Proton-Translocating ATPases - chemistry Saccharomyces cerevisiae - metabolism spermine Spodoptera transporter |
Title | Structural basis of polyamine transport by human ATP13A2 (PARK9) |
URI | https://dx.doi.org/10.1016/j.molcel.2021.08.017 https://www.ncbi.nlm.nih.gov/pubmed/34715013 https://search.proquest.com/docview/2590137533 https://pubmed.ncbi.nlm.nih.gov/PMC8604775 |
Volume | 81 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB61WyFxQbzZApWROMDB2sSP2L6RVlSFAqpoi_Zm2YktFrXJSt0e9t_jyWPFAhISx_ihWDPOzEQz3zcAr42OXjBlqIyspkJpQ30WA2XcBZluSCE8Apw_fylOLsXHuZzvwNGIhcGyysH29za9s9bDyGyQ5my5WMzOMXfKVJH8D-IchNyFPYZppgnslYffTj9tkglCdp3wcD3FDSOCrivzum6vqoA5CNZzeXady_7qof6MQH8vpPzFMx3fh3tDSEnK_tQPYCc0D-FO32Ry_QjenXcUsUivQZLPWtyQNpJle7V21ynCJKuR3Zz4Nek69pHy4iznJSNvzsqvp-btY7g8fn9xdEKHvgm0ksysqPFaO-28kSKGoHTGuVe1K1jtHGLflak9r3Xugs5C5iulQxWcYXXOQ8Ss_BOYNG0TngGJLEQuVUCbKWSsnEoBXmW4S4NV7s0U6Cgru-zpMexYN_bD9rK1KFuLzS5zNQU1CtRuqdkmC_6Pna9G-dv0BWBawzWhvb2xDOGzPP128Sk87fWxOQtPvlem2fTeLU1tFiC79vZMs_jesWzrIhNKyf3_PvFzuItPCFzM9QuYJGWHlymCWfmD4YYewO6H-eFPNZHvwQ |
link.rule.ids | 230,315,786,790,891,3525,27600,27955,27956,45696,45907 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LTxsxELYoCLWXCkofaQt1JQ7twcquH2v71gUVhSYgVELFzbJ3bTUV7EYiPeTf17OPiNBKlbj6obVm7JlZzXzfIHSoVXCcSk1EoCXhUmnikuAJZdaLeEMy7gDgfHaeja74t2txvYGOeywMlFV2tr-16Y217kaGnTSH89lseAm5Uyqz6H8A58DFE7QVowEdr_lWfvRjPFklE7hoOuHBegIbegRdU-Z1W98UHnIQtOXybDqX_dND_R2BPiykvOeZTnbQ8y6kxHl76l204asXaLttMrncQ18uG4pYoNfA0WfN7nAd8Ly-WdrbGGHiRc9ujt0SNx37cD69SFlO8aeL_PtYf36Jrk6-To9HpOubQApB9YJop5RV1mnBg_dSJYw5WdqMltYC9l3q0rFSpdarxCeukMoX3mpapswHyMq_QptVXfk3CAfqAxPSg83kIhRWxgCv0MzGwSJ1eoBILyszb-kxTF839su0sjUgWwPNLlM5QLIXqFlTs4kW_D87P_byN_EFQFrDVr7-fWcowGdZ_O1iA_S61cfqLCz6XhFn43fXNLVaAOza6zPV7GfDsq2yhEsp3j76xB_Q09H0bGImp-fjd-gZzACIMVXv0WZUvN-P0czCHXS39Q8ULvG2 |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Structural+basis+of+polyamine+transport+by+human+ATP13A2+%28PARK9%29&rft.jtitle=Molecular+cell&rft.au=Sim%2C+Sue+Im&rft.au=von+B%C3%BClow%2C+S%C3%B6ren&rft.au=Hummer%2C+Gerhard&rft.au=Park%2C+Eunyong&rft.date=2021-11-18&rft.issn=1097-2765&rft.eissn=1097-4164&rft.volume=81&rft.issue=22&rft.spage=4635&rft.epage=4649.e8&rft_id=info:doi/10.1016%2Fj.molcel.2021.08.017&rft_id=info%3Apmid%2F34715013&rft.externalDBID=PMC8604775 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1097-2765&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1097-2765&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1097-2765&client=summon |