The Mammalian Brain rsec6/8 Complex
rsec6 and rsec8 are two components of a 17S complex in mammalian brain that is homologous to the yeast 834 kDa Sec6/8/15 complex which is essential for exocytosis. Purification and partial amino acid sequencing of the mammalian rsec6/8 complex reveals that it is composed of eight novel proteins with...
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Published in | Neuron (Cambridge, Mass.) Vol. 17; no. 6; pp. 1209 - 1219 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.12.1996
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Subjects | |
Online Access | Get full text |
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Abstract | rsec6 and rsec8 are two components of a 17S complex in mammalian brain that is homologous to the yeast 834 kDa Sec6/8/15 complex which is essential for exocytosis. Purification and partial amino acid sequencing of the mammalian rsec6/8 complex reveals that it is composed of eight novel proteins with a combined molecular weight of 743 kDa. The complex is broadly expressed in brain and displays a plasma membrane localization in nerve terminals. Membrane associated rsec6/8 complex coimmunoprecipitates with syntaxin, a plasma membrane protein critical for neurotransmission. These data suggest a role for the mammalian rsec6/8 complex in neurotransmitter release via interactions with the core vesicle docking and fusion apparatus. |
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AbstractList | rsec6 and rsec8 are two components of a 17S complex in mammalian brain that is homologous to the yeast 834 kDa Sec6/8/15 complex which is essential for exocytosis. Purification and partial amino acid sequencing of the mammalian rsec6/8 complex reveals that it is composed of eight novel proteins with a combined molecular weight of 743 kDa. The complex is broadly expressed in brain and displays a plasma membrane localization in nerve terminals. Membrane associated rsec6/8 complex coimmunoprecipitates with syntaxin, a plasma membrane protein critical for neurotransmission. These data suggest a role for the mammalian rsec6/8 complex in neurotransmitter release via interactions with the core vesicle docking and fusion apparatus. Rse6 and rsec8 are two components of a 17S complex in mammalian brain that is homologous to the yeast 834 kDa Sec6/8/15 complex which is essential for exocytosis. Purification and partial amino acid sequencing of the mammalian rsec6/8 complex reveals that it is composed of eight novel proteins with a combined molecular weight of 743 kDa. The complex is broadly expressed in brain and displays a plasma membrane localization in nerve terminals. Membrane associated rsec6/8 complex coimmunoprecipitates with syntaxin, a plasma membrane protein critical for neurotransmission. These data suggest a role for the mammalian rsec6/8 complex in neurotransmitter release via interactions with the core vesicle docking and fusion apparatus. |
Author | Kee, Yun Hazuka, Christopher D Davanger, Svend Scheller, Richard H Hsu, Shu-Chan Ting, Anthony E Kenny, James W |
Author_xml | – sequence: 1 givenname: Shu-Chan surname: Hsu fullname: Hsu, Shu-Chan organization: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305-5428, USA – sequence: 2 givenname: Anthony E surname: Ting fullname: Ting, Anthony E organization: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305-5428, USA – sequence: 3 givenname: Christopher D surname: Hazuka fullname: Hazuka, Christopher D organization: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305-5428, USA – sequence: 4 givenname: Svend surname: Davanger fullname: Davanger, Svend organization: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305-5428, USA – sequence: 5 givenname: James W surname: Kenny fullname: Kenny, James W organization: Hewlett-Packard Company, California Analytical Division, 1601 California Avenue, Palo Alto, California 94034, USA – sequence: 6 givenname: Yun surname: Kee fullname: Kee, Yun organization: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305-5428, USA – sequence: 7 givenname: Richard H surname: Scheller fullname: Scheller, Richard H email: scheller@cmgm.stanford.edu organization: Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305-5428, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8982167$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1038/375645a0 10.1083/jcb.116.3.761 10.1073/pnas.89.10.4338 10.1083/jcb.57.2.315 10.1126/science.8430330 10.1083/jcb.118.5.1041 10.1016/0896-6273(94)90352-2 10.1038/372055a0 10.1038/326498a0 10.1016/0898-6568(89)90051-X 10.1083/jcb.119.1.139 10.1038/370191a0 10.1073/pnas.91.4.1445 10.1038/362560a0 10.1083/jcb.128.4.589 10.1016/0896-6273(95)90328-3 10.1073/pnas.91.6.1987 10.1083/jcb.109.3.1023 10.1073/pnas.88.14.6196 10.1016/0896-6273(94)90443-X 10.1083/jcb.130.5.1105 10.1038/362318a0 10.1073/pnas.87.5.1988 10.1016/0076-6879(86)21017-4 10.1111/j.1749-6632.1994.tb17275.x 10.1073/pnas.90.7.2559 10.1038/357134a0 10.1083/jcb.130.2.299 10.1073/pnas.92.21.9613 10.1002/j.1460-2075.1993.tb06093.x 10.1016/0092-8674(93)90376-2 10.1016/S0378-4347(96)00230-7 10.1083/jcb.100.4.1284 10.1016/0092-8674(80)90128-2 10.1126/science.1321498 10.1016/0014-5793(86)81049-3 |
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References | Lelkes, Friedman, Rosenheck, Oplatka (BIB32) 1986; 208 Bennett, Calakos, Kreiner, Scheller (BIB4) 1992; 116 Burgoyne, Morgan, O'Sullivan (BIB28) 1989; 1 Perrin, Langley, Aunis (BIB35) 1987; 326 Mays, Siemers, Fritz, Lowe, van Meer, Nelson (BIB16) 1995; 130 Söllner, Whiteheart, Brunner, Erdjument-Bromage, Geromanos, Tempst, Rothman (BIB24) 1993; 362 Rothman (BIB21) 1994; 372 Pevsner, Hsu, Scheller (BIB19) 1994; 91 Ting, Hazuka, Hsu, Kirk, Bean, Scheller (BIB27) 1995; 92 Heuser, Reese (BIB13) 1973; 57 Aalto, Ronne, Keränen (BIB1) 1993; 12 TerBush, Novick (BIB26) 1995; 130 Buckley, Kelly (BIB8) 1985; 100 Bennett, Calakos, Scheller (BIB5) 1992; 257 Greengard, Valtorta, Czernik, Benfenati (BIB29) 1993; 259 Bennett, Scheller (BIB3) 1993; 90 Fischer von Mollard, Mignery, Baumert, Perin, Hanson, Burger, Jahn, Südhof (BIB11) 1990; 87 Gerst, Rodgers, Riggs, Wigler (BIB12) 1992; 89 Scheller (BIB22) 1995; 14 Malgaroli, Tsien (BIB33) 1992; 357 Hwang, Smith, Chu (BIB14) 1996 Hay, Martin (BIB30) 1992; 119 Bowser, Müller, Govindan, Novick (BIB6) 1992; 118 Lane, Crissman, Ginn (BIB15) 1986; 121 Pevsner, Hsu, Braun, Calakos, Ting, Bennett, Scheller (BIB18) 1994; 13 Hunt, Bommert, Charlton, Kistner, Habermann, Augustine, Betz (BIB31) 1994; 12 Bennett (BIB2) 1994; 733 Südhof (BIB25) 1995; 375 Novick, Field, Schekman (BIB17) 1980; 21 Sontag, Aunis, Bader (BIB37) 1988; 46 Ferro-Novick, Jahn (BIB10) 1994; 370 Brennwald, Novick (BIB7) 1993; 362 Pfeffer (BIB20) 1994; 91 Söllner, Bennett, Whiteheart, Scheller, Rothman (BIB23) 1993; 75 Muallem, Kwiatkowska, Xu, Yin (BIB34) 1995; 128 Farnsworth, Kawata, Yoshida, Takai, Gelb, Glomset (BIB9) 1991; 88 Salminen, Novick (BIB36) 1989; 109 Bennett (10.1016/S0896-6273(00)80251-2_BIB5) 1992; 257 Hwang (10.1016/S0896-6273(00)80251-2_BIB14) 1996 Bennett (10.1016/S0896-6273(00)80251-2_BIB3) 1993; 90 Malgaroli (10.1016/S0896-6273(00)80251-2_BIB33) 1992; 357 Heuser (10.1016/S0896-6273(00)80251-2_BIB13) 1973; 57 Pfeffer (10.1016/S0896-6273(00)80251-2_BIB20) 1994; 91 Südhof (10.1016/S0896-6273(00)80251-2_BIB25) 1995; 375 Hay (10.1016/S0896-6273(00)80251-2_BIB30) 1992; 119 Fischer von Mollard (10.1016/S0896-6273(00)80251-2_BIB11) 1990; 87 Brennwald (10.1016/S0896-6273(00)80251-2_BIB7) 1993; 362 Mays (10.1016/S0896-6273(00)80251-2_BIB16) 1995; 130 Scheller (10.1016/S0896-6273(00)80251-2_BIB22) 1995; 14 Muallem (10.1016/S0896-6273(00)80251-2_BIB34) 1995; 128 Gerst (10.1016/S0896-6273(00)80251-2_BIB12) 1992; 89 Ting (10.1016/S0896-6273(00)80251-2_BIB27) 1995; 92 Lane (10.1016/S0896-6273(00)80251-2_BIB15) 1986; 121 Salminen (10.1016/S0896-6273(00)80251-2_BIB36) 1989; 109 Söllner (10.1016/S0896-6273(00)80251-2_BIB23) 1993; 75 Burgoyne (10.1016/S0896-6273(00)80251-2_BIB28) 1989; 1 Pevsner (10.1016/S0896-6273(00)80251-2_BIB19) 1994; 91 Pevsner (10.1016/S0896-6273(00)80251-2_BIB18) 1994; 13 Bowser (10.1016/S0896-6273(00)80251-2_BIB6) 1992; 118 Novick (10.1016/S0896-6273(00)80251-2_BIB17) 1980; 21 Buckley (10.1016/S0896-6273(00)80251-2_BIB8) 1985; 100 Farnsworth (10.1016/S0896-6273(00)80251-2_BIB9) 1991; 88 Bennett (10.1016/S0896-6273(00)80251-2_BIB2) 1994; 733 Perrin (10.1016/S0896-6273(00)80251-2_BIB35) 1987; 326 Sontag (10.1016/S0896-6273(00)80251-2_BIB37) 1988; 46 Rothman (10.1016/S0896-6273(00)80251-2_BIB21) 1994; 372 Greengard (10.1016/S0896-6273(00)80251-2_BIB29) 1993; 259 Söllner (10.1016/S0896-6273(00)80251-2_BIB24) 1993; 362 TerBush (10.1016/S0896-6273(00)80251-2_BIB26) 1995; 130 Bennett (10.1016/S0896-6273(00)80251-2_BIB4) 1992; 116 Hunt (10.1016/S0896-6273(00)80251-2_BIB31) 1994; 12 Aalto (10.1016/S0896-6273(00)80251-2_BIB1) 1993; 12 Ferro-Novick (10.1016/S0896-6273(00)80251-2_BIB10) 1994; 370 Lelkes (10.1016/S0896-6273(00)80251-2_BIB32) 1986; 208 |
References_xml | – volume: 357 start-page: 134 year: 1992 end-page: 139 ident: BIB33 article-title: Glutamate-induced long-term potentiation of the frequency of miniature synaptic currents in cultured hippocampal neurons publication-title: Nature contributor: fullname: Tsien – volume: 372 start-page: 55 year: 1994 end-page: 63 ident: BIB21 article-title: Mechanisms of intracellular protein transport publication-title: Nature contributor: fullname: Rothman – volume: 12 start-page: 4095 year: 1993 end-page: 4104 ident: BIB1 article-title: Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport publication-title: EMBO J contributor: fullname: Keränen – volume: 12 start-page: 1269 year: 1994 end-page: 1279 ident: BIB31 article-title: A post-docking role for synaptobrevin in synaptic vesicle fusion publication-title: Neuron contributor: fullname: Betz – volume: 87 start-page: 1988 year: 1990 end-page: 1992 ident: BIB11 article-title: Rab3A is a small GTP-binding protein exclusively localized to synaptic vesicles publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Südhof – year: 1996 ident: BIB14 article-title: Internal sequence analysis of proteins eluted from polyacrylamide gels publication-title: J. Chromatogr. B. Biomed. Appl., in press contributor: fullname: Chu – volume: 121 start-page: 183 year: 1986 end-page: 192 ident: BIB15 article-title: High efficiency fusion procedure for producing monoclonal antibodies against weak immunogens publication-title: Meth. Enzymol contributor: fullname: Ginn – volume: 118 start-page: 1041 year: 1992 end-page: 1056 ident: BIB6 article-title: Sec8p and Sec15p are components of a plasma membrane–associated 19.5S particle that may function downstream of Sec4p to control exocytosis publication-title: J. Cell Biol contributor: fullname: Novick – volume: 46 start-page: 316 year: 1988 end-page: 326 ident: BIB37 article-title: Peripheral actin filaments control calcium-mediated catecholamine release from streptolysin-O-Permeabilized chromaffin cells publication-title: Eur. J. Cell Biol contributor: fullname: Bader – volume: 14 start-page: 893 year: 1995 end-page: 897 ident: BIB22 article-title: Membrane trafficking in the presynaptic nerve terminal publication-title: Neuron contributor: fullname: Scheller – volume: 88 start-page: 6196 year: 1991 end-page: 6200 ident: BIB9 article-title: C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Glomset – volume: 91 start-page: 1987 year: 1994 end-page: 1988 ident: BIB20 article-title: Clues to brain function from bakers' yeast publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Pfeffer – volume: 362 start-page: 318 year: 1993 end-page: 324 ident: BIB24 article-title: SNAP receptors implicated in vesicle targeting and fusion publication-title: Nature contributor: fullname: Rothman – volume: 128 start-page: 589 year: 1995 end-page: 598 ident: BIB34 article-title: Actin filament disassembly is a sufficient final trigger for exocytosis in non-excitable cells publication-title: J. Cell Biol contributor: fullname: Yin – volume: 90 start-page: 2559 year: 1993 end-page: 2563 ident: BIB3 article-title: The molecular machinery for secretion is conserved from yeast to neurons publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Scheller – volume: 89 start-page: 4338 year: 1992 end-page: 4342 ident: BIB12 article-title: SNC1, a yeast homolog of the synaptic vesicle–associated membrane protein/synaptobrevin gene family publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Wigler – volume: 733 start-page: 256 year: 1994 end-page: 265 ident: BIB2 article-title: Molecular mechanisms of neurotransmitter release publication-title: Ann. NY Acad. Sci contributor: fullname: Bennett – volume: 208 start-page: 357 year: 1986 end-page: 363 ident: BIB32 article-title: Destabilization of actin filaments as a requirement for the secretion of catecholamines from permeabilized chromaffin cells publication-title: FEBS Lett contributor: fullname: Oplatka – volume: 370 start-page: 191 year: 1994 end-page: 193 ident: BIB10 article-title: Vesicle fusion from yeast to man publication-title: Nature contributor: fullname: Jahn – volume: 119 start-page: 139 year: 1992 end-page: 151 ident: BIB30 article-title: Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins publication-title: J. Cell Biol contributor: fullname: Martin – volume: 57 start-page: 315 year: 1973 end-page: 344 ident: BIB13 article-title: Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction publication-title: J. Cell Biol contributor: fullname: Reese – volume: 130 start-page: 1105 year: 1995 end-page: 1115 ident: BIB16 article-title: Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells publication-title: J. Cell Biol contributor: fullname: Nelson – volume: 91 start-page: 1445 year: 1994 end-page: 1449 ident: BIB19 article-title: n-Sec1 publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Scheller – volume: 92 start-page: 9613 year: 1995 end-page: 9617 ident: BIB27 article-title: rSec6 and rSec8, mammalian homologs of yeast proteins essential for secretion publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Scheller – volume: 1 start-page: 323 year: 1989 end-page: 334 ident: BIB28 article-title: The control of cytoskeletal actin and exocytosis in intact and permeabilized adrenal chromaffin cells publication-title: Cell. Signaling contributor: fullname: O'Sullivan – volume: 116 start-page: 761 year: 1992 end-page: 775 ident: BIB4 article-title: Synaptic vesicle membrane proteins interact to form a multimeric complex publication-title: J. Cell Biol contributor: fullname: Scheller – volume: 257 start-page: 255 year: 1992 end-page: 259 ident: BIB5 article-title: Syntaxin publication-title: Science contributor: fullname: Scheller – volume: 259 start-page: 780 year: 1993 end-page: 785 ident: BIB29 article-title: Synaptic vesicle phosphoproteins and regulation of synaptic function publication-title: Science contributor: fullname: Benfenati – volume: 21 start-page: 205 year: 1980 end-page: 215 ident: BIB17 article-title: Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway publication-title: Cell contributor: fullname: Schekman – volume: 362 start-page: 560 year: 1993 end-page: 563 ident: BIB7 article-title: Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4 publication-title: Nature contributor: fullname: Novick – volume: 109 start-page: 1023 year: 1989 end-page: 1036 ident: BIB36 article-title: The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast publication-title: J. Cell Biol contributor: fullname: Novick – volume: 75 start-page: 409 year: 1993 end-page: 418 ident: BIB23 article-title: A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion publication-title: Cell contributor: fullname: Rothman – volume: 13 start-page: 353 year: 1994 end-page: 361 ident: BIB18 article-title: Specificity and regulation of a synaptic vesicle docking complex publication-title: Neuron contributor: fullname: Scheller – volume: 326 start-page: 498 year: 1987 end-page: 501 ident: BIB35 article-title: Anti-α-fodrin inhibits secretion from permeabilized chromaffin cells publication-title: Nature contributor: fullname: Aunis – volume: 100 start-page: 1284 year: 1985 end-page: 1294 ident: BIB8 article-title: Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells publication-title: J. Cell Biol contributor: fullname: Kelly – volume: 375 start-page: 645 year: 1995 end-page: 653 ident: BIB25 article-title: The synaptic vesicle cycle publication-title: Nature contributor: fullname: Südhof – volume: 130 start-page: 299 year: 1995 end-page: 312 ident: BIB26 article-title: Sec6, Sec8 and Sec15 are components of a multisubunit complex which localizes to small bud tips in publication-title: J. Cell Biol contributor: fullname: Novick – volume: 375 start-page: 645 year: 1995 ident: 10.1016/S0896-6273(00)80251-2_BIB25 article-title: The synaptic vesicle cycle publication-title: Nature doi: 10.1038/375645a0 contributor: fullname: Südhof – volume: 116 start-page: 761 year: 1992 ident: 10.1016/S0896-6273(00)80251-2_BIB4 article-title: Synaptic vesicle membrane proteins interact to form a multimeric complex publication-title: J. Cell Biol doi: 10.1083/jcb.116.3.761 contributor: fullname: Bennett – volume: 89 start-page: 4338 year: 1992 ident: 10.1016/S0896-6273(00)80251-2_BIB12 article-title: SNC1, a yeast homolog of the synaptic vesicle–associated membrane protein/synaptobrevin gene family publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.89.10.4338 contributor: fullname: Gerst – volume: 57 start-page: 315 year: 1973 ident: 10.1016/S0896-6273(00)80251-2_BIB13 article-title: Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction publication-title: J. Cell Biol doi: 10.1083/jcb.57.2.315 contributor: fullname: Heuser – volume: 259 start-page: 780 year: 1993 ident: 10.1016/S0896-6273(00)80251-2_BIB29 article-title: Synaptic vesicle phosphoproteins and regulation of synaptic function publication-title: Science doi: 10.1126/science.8430330 contributor: fullname: Greengard – volume: 118 start-page: 1041 year: 1992 ident: 10.1016/S0896-6273(00)80251-2_BIB6 article-title: Sec8p and Sec15p are components of a plasma membrane–associated 19.5S particle that may function downstream of Sec4p to control exocytosis publication-title: J. Cell Biol doi: 10.1083/jcb.118.5.1041 contributor: fullname: Bowser – volume: 13 start-page: 353 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB18 article-title: Specificity and regulation of a synaptic vesicle docking complex publication-title: Neuron doi: 10.1016/0896-6273(94)90352-2 contributor: fullname: Pevsner – volume: 372 start-page: 55 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB21 article-title: Mechanisms of intracellular protein transport publication-title: Nature doi: 10.1038/372055a0 contributor: fullname: Rothman – volume: 46 start-page: 316 year: 1988 ident: 10.1016/S0896-6273(00)80251-2_BIB37 article-title: Peripheral actin filaments control calcium-mediated catecholamine release from streptolysin-O-Permeabilized chromaffin cells publication-title: Eur. J. Cell Biol contributor: fullname: Sontag – volume: 326 start-page: 498 year: 1987 ident: 10.1016/S0896-6273(00)80251-2_BIB35 article-title: Anti-α-fodrin inhibits secretion from permeabilized chromaffin cells publication-title: Nature doi: 10.1038/326498a0 contributor: fullname: Perrin – volume: 1 start-page: 323 year: 1989 ident: 10.1016/S0896-6273(00)80251-2_BIB28 article-title: The control of cytoskeletal actin and exocytosis in intact and permeabilized adrenal chromaffin cells publication-title: Cell. Signaling doi: 10.1016/0898-6568(89)90051-X contributor: fullname: Burgoyne – volume: 119 start-page: 139 year: 1992 ident: 10.1016/S0896-6273(00)80251-2_BIB30 article-title: Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins publication-title: J. Cell Biol doi: 10.1083/jcb.119.1.139 contributor: fullname: Hay – volume: 370 start-page: 191 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB10 article-title: Vesicle fusion from yeast to man publication-title: Nature doi: 10.1038/370191a0 contributor: fullname: Ferro-Novick – volume: 91 start-page: 1445 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB19 article-title: n-Sec1 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.91.4.1445 contributor: fullname: Pevsner – volume: 362 start-page: 560 year: 1993 ident: 10.1016/S0896-6273(00)80251-2_BIB7 article-title: Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4 publication-title: Nature doi: 10.1038/362560a0 contributor: fullname: Brennwald – volume: 128 start-page: 589 year: 1995 ident: 10.1016/S0896-6273(00)80251-2_BIB34 article-title: Actin filament disassembly is a sufficient final trigger for exocytosis in non-excitable cells publication-title: J. Cell Biol doi: 10.1083/jcb.128.4.589 contributor: fullname: Muallem – volume: 14 start-page: 893 year: 1995 ident: 10.1016/S0896-6273(00)80251-2_BIB22 article-title: Membrane trafficking in the presynaptic nerve terminal publication-title: Neuron doi: 10.1016/0896-6273(95)90328-3 contributor: fullname: Scheller – volume: 91 start-page: 1987 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB20 article-title: Clues to brain function from bakers' yeast publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.91.6.1987 contributor: fullname: Pfeffer – volume: 109 start-page: 1023 year: 1989 ident: 10.1016/S0896-6273(00)80251-2_BIB36 article-title: The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast publication-title: J. Cell Biol doi: 10.1083/jcb.109.3.1023 contributor: fullname: Salminen – volume: 88 start-page: 6196 year: 1991 ident: 10.1016/S0896-6273(00)80251-2_BIB9 article-title: C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.88.14.6196 contributor: fullname: Farnsworth – volume: 12 start-page: 1269 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB31 article-title: A post-docking role for synaptobrevin in synaptic vesicle fusion publication-title: Neuron doi: 10.1016/0896-6273(94)90443-X contributor: fullname: Hunt – volume: 130 start-page: 1105 year: 1995 ident: 10.1016/S0896-6273(00)80251-2_BIB16 article-title: Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells publication-title: J. Cell Biol doi: 10.1083/jcb.130.5.1105 contributor: fullname: Mays – volume: 362 start-page: 318 year: 1993 ident: 10.1016/S0896-6273(00)80251-2_BIB24 article-title: SNAP receptors implicated in vesicle targeting and fusion publication-title: Nature doi: 10.1038/362318a0 contributor: fullname: Söllner – volume: 87 start-page: 1988 year: 1990 ident: 10.1016/S0896-6273(00)80251-2_BIB11 article-title: Rab3A is a small GTP-binding protein exclusively localized to synaptic vesicles publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.87.5.1988 contributor: fullname: Fischer von Mollard – volume: 121 start-page: 183 year: 1986 ident: 10.1016/S0896-6273(00)80251-2_BIB15 article-title: High efficiency fusion procedure for producing monoclonal antibodies against weak immunogens publication-title: Meth. Enzymol doi: 10.1016/0076-6879(86)21017-4 contributor: fullname: Lane – volume: 733 start-page: 256 year: 1994 ident: 10.1016/S0896-6273(00)80251-2_BIB2 article-title: Molecular mechanisms of neurotransmitter release publication-title: Ann. NY Acad. Sci doi: 10.1111/j.1749-6632.1994.tb17275.x contributor: fullname: Bennett – volume: 90 start-page: 2559 year: 1993 ident: 10.1016/S0896-6273(00)80251-2_BIB3 article-title: The molecular machinery for secretion is conserved from yeast to neurons publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.90.7.2559 contributor: fullname: Bennett – volume: 357 start-page: 134 year: 1992 ident: 10.1016/S0896-6273(00)80251-2_BIB33 article-title: Glutamate-induced long-term potentiation of the frequency of miniature synaptic currents in cultured hippocampal neurons publication-title: Nature doi: 10.1038/357134a0 contributor: fullname: Malgaroli – volume: 130 start-page: 299 year: 1995 ident: 10.1016/S0896-6273(00)80251-2_BIB26 article-title: Sec6, Sec8 and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae publication-title: J. Cell Biol doi: 10.1083/jcb.130.2.299 contributor: fullname: TerBush – volume: 92 start-page: 9613 year: 1995 ident: 10.1016/S0896-6273(00)80251-2_BIB27 article-title: rSec6 and rSec8, mammalian homologs of yeast proteins essential for secretion publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.92.21.9613 contributor: fullname: Ting – volume: 12 start-page: 4095 year: 1993 ident: 10.1016/S0896-6273(00)80251-2_BIB1 article-title: Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport publication-title: EMBO J doi: 10.1002/j.1460-2075.1993.tb06093.x contributor: fullname: Aalto – volume: 75 start-page: 409 year: 1993 ident: 10.1016/S0896-6273(00)80251-2_BIB23 article-title: A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion publication-title: Cell doi: 10.1016/0092-8674(93)90376-2 contributor: fullname: Söllner – year: 1996 ident: 10.1016/S0896-6273(00)80251-2_BIB14 article-title: Internal sequence analysis of proteins eluted from polyacrylamide gels publication-title: J. Chromatogr. B. Biomed. Appl., in press doi: 10.1016/S0378-4347(96)00230-7 contributor: fullname: Hwang – volume: 100 start-page: 1284 year: 1985 ident: 10.1016/S0896-6273(00)80251-2_BIB8 article-title: Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells publication-title: J. Cell Biol doi: 10.1083/jcb.100.4.1284 contributor: fullname: Buckley – volume: 21 start-page: 205 year: 1980 ident: 10.1016/S0896-6273(00)80251-2_BIB17 article-title: Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway publication-title: Cell doi: 10.1016/0092-8674(80)90128-2 contributor: fullname: Novick – volume: 257 start-page: 255 year: 1992 ident: 10.1016/S0896-6273(00)80251-2_BIB5 article-title: Syntaxin publication-title: Science doi: 10.1126/science.1321498 contributor: fullname: Bennett – volume: 208 start-page: 357 year: 1986 ident: 10.1016/S0896-6273(00)80251-2_BIB32 article-title: Destabilization of actin filaments as a requirement for the secretion of catecholamines from permeabilized chromaffin cells publication-title: FEBS Lett doi: 10.1016/0014-5793(86)81049-3 contributor: fullname: Lelkes |
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Snippet | rsec6 and rsec8 are two components of a 17S complex in mammalian brain that is homologous to the yeast 834 kDa Sec6/8/15 complex which is essential for... Rse6 and rsec8 are two components of a 17S complex in mammalian brain that is homologous to the yeast 834 kDa Sec6/8/15 complex which is essential for... |
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SubjectTerms | Animals Brain - metabolism Carrier Proteins Cells, Cultured Hippocampus - cytology Hippocampus - metabolism Mammalia Membrane Proteins - metabolism Neurons - metabolism Peptide Mapping Precipitin Tests Proteins - genetics Proteins - isolation & purification Proteins - metabolism Qa-SNARE Proteins Rats Subcellular Fractions - metabolism Tissue Distribution |
Title | The Mammalian Brain rsec6/8 Complex |
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