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Volumn 145, Issue 7, 1999, Pages 1435-1442

Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion

Author keywords

SNAP; Membrane fusion; NSF; SNAREs; Yeast vacuoles

Indexed keywords

MEMBRANE PROTEIN;

EID: 0344052673     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.145.7.1435     Document Type: Article
Times cited : (136)

References (62)
  • 1
    • 0029024860 scopus 로고
    • A SNARE-like protein required for traffic through the Golgi complex
    • Banfield, D.K., M.J. Lewis, and H.R.B. Pelham. 1995. A SNARE-like protein required for traffic through the Golgi complex. Nature. 375:806-809.
    • (1995) Nature , vol.375 , pp. 806-809
    • Banfield, D.K.1    Lewis, M.J.2    Pelham, H.R.B.3
  • 2
    • 0031854866 scopus 로고    scopus 로고
    • Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment
    • Bryant, N., R.C. Piper, L.S. Weissman, and T.H. Stevens. 1998. Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment. J. Cell Biol. 142:651-663.
    • (1998) J. Cell Biol. , vol.142 , pp. 651-663
    • Bryant, N.1    Piper, R.C.2    Weissman, L.S.3    Stevens, T.H.4
  • 3
    • 0030952211 scopus 로고    scopus 로고
    • A novel Sec18p/ NSF-dependent complex required for Golgi-to-endosome transport in yeast
    • Burd, C.G., M. Peterson, C.R. Cowles, and S.D. Emr. 1997. A novel Sec18p/ NSF-dependent complex required for Golgi-to-endosome transport in yeast. Mol. Biol. Cell. 8:1089-1104.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1089-1104
    • Burd, C.G.1    Peterson, M.2    Cowles, C.R.3    Emr, S.D.4
  • 4
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., N. Ballew, and C. Barlowe. 1998. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO (Eur. Mol. Biol. Org.) J. 17:2156-2165.
    • (1998) EMBO (Eur. Mol. Biol. Org.) J. , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 5
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosomal docking
    • Christoforidis, S., H.M. McBride, R.D. Burgoyne, and M. Zerial. 1999. The Rab5 effector EEA1 is a core component of endosomal docking. Nature. 397:621-625.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 6
    • 0027093271 scopus 로고
    • In vitro reactions of vacuole inheritance in Saccharomyces cerevisiae
    • Conradt, B., J. Shaw, T. Vida, S.D. Emr, and W. Wickner. 1992. In vitro reactions of vacuole inheritance in Saccharomyces cerevisiae. J Cell Biol. 119: 1469-1479.
    • (1992) J Cell Biol. , vol.119 , pp. 1469-1479
    • Conradt, B.1    Shaw, J.2    Vida, T.3    Emr, S.D.4    Wickner, W.5
  • 7
    • 0032576575 scopus 로고    scopus 로고
    • Biochemical and functional studies of cortical vesicle fusion: The SNARE complex and Ca2+ sensitivity
    • Coorssen, J.R., P.S. Blank, M. Tahara, and J. Zimmerberg. 1998. Biochemical and functional studies of cortical vesicle fusion: the SNARE complex and Ca2+ sensitivity. J. Cell Biol. 143:1845-1857.
    • (1998) J. Cell Biol. , vol.143 , pp. 1845-1857
    • Coorssen, J.R.1    Blank, P.S.2    Tahara, M.3    Zimmerberg, J.4
  • 8
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles, C.R., G. Odorizzi, G.S. Payne, and S.D. Emr. 1997. The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell. 91:109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 9
    • 0030807624 scopus 로고    scopus 로고
    • A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
    • Darsow, T., S.E. Rieder, and S.D. Emr. 1997. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J. Cell Biol. 138:517-529.
    • (1997) J. Cell Biol. , vol.138 , pp. 517-529
    • Darsow, T.1    Rieder, S.E.2    Emr, S.D.3
  • 10
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs
    • Fasshauer, D., R.B. Sutton, A.T. Brunger, and R. Jahn. 1998. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs. Proc. Nat. Acad. Sci. USA. 95:15781-15786.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 11
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick, S., and R. Jahn. 1994. Vesicle fusion from yeast to man. Nature. 370:191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 12
    • 0001206086 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole
    • Fischer von Mollard, G., and T.H. Stevens. 1999. The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. Mol. Biol. Cell. 10:1719-1732.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1719-1732
    • Fischer Von Mollard, G.1    Stevens, T.H.2
  • 13
    • 0030990122 scopus 로고    scopus 로고
    • The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p
    • Fischer von Mollard, G., S. Notwehr, and T.H. Stevens. 1997. The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. J. Cell Biol. 137:1511-1524.
    • (1997) J. Cell Biol. , vol.137 , pp. 1511-1524
    • Fischer Von Mollard, G.1    Notwehr, S.2    Stevens, T.H.3
  • 14
    • 0242546913 scopus 로고    scopus 로고
    • High expression of the yeast syntaxin-related Vam3 protein suppresses the protein transport defects of a pep12 null mutant
    • Götte, M., and D. Gallwitz. 1997. High expression of the yeast syntaxin-related Vam3 protein suppresses the protein transport defects of a pep12 null mutant. FEBS Lett. 411:48-52.
    • (1997) FEBS Lett. , vol.411 , pp. 48-52
    • Götte, M.1    Gallwitz, D.2
  • 15
    • 0001199243 scopus 로고
    • A quantitative assay to measure homotypic vacuole fusion in vitro
    • Haas, A. 1995. A quantitative assay to measure homotypic vacuole fusion in vitro. Meth. Cell Sci. 17:283-294.
    • (1995) Meth. Cell Sci. , vol.17 , pp. 283-294
    • Haas, A.1
  • 16
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuole fusion requires Sec17p (yeast α-SNAP) and Sec18p (yeast NSF)
    • Haas, A., and W. Wickner. 1996. Homotypic vacuole fusion requires Sec17p (yeast α-SNAP) and Sec18p (yeast NSF). EMBO (Eur. Mol. Biol. Org.) J. 15:3296-3305.
    • (1996) EMBO (Eur. Mol. Biol. Org.) J. , vol.15 , pp. 3296-3305
    • Haas, A.1    Wickner, W.2
  • 17
    • 0028333056 scopus 로고
    • G-protein ligands inhibit in vitro reactions of vacuole inheritance
    • Haas, A., B. Conradt, and W. Wickner. 1994. G-protein ligands inhibit in vitro reactions of vacuole inheritance. J. Cell Biol. 126:87-97.
    • (1994) J. Cell Biol. , vol.126 , pp. 87-97
    • Haas, A.1    Conradt, B.2    Wickner, W.3
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Harlow, E., and O. Lane. 1988. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. 519-551.
    • (1988) Antibodies: A Laboratory Manual , pp. 519-551
    • Harlow, E.1    Lane, O.2
  • 19
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J.C., and R. Scheller. 1997. SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9:505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.2
  • 23
    • 0029808148 scopus 로고    scopus 로고
    • Delayed extraction improves specificity in database searches by MALDI peptide maps
    • Jensen, O.N., A.V. Podtelejnikov, and M. Mann. 1996. Delayed extraction improves specificity in database searches by MALDI peptide maps. Rapid Commun. Mass Spectrom. 10:1371-1378.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1371-1378
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 24
    • 0031298696 scopus 로고    scopus 로고
    • Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching
    • Jensen, O.N., A.V. Podtelejnikov, and M. Mann. 1997. Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal. Chem. 69:4741-4750.
    • (1997) Anal. Chem. , vol.69 , pp. 4741-4750
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 25
    • 0032253972 scopus 로고    scopus 로고
    • Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: Strategies and applications
    • Jensen, O.N., M.R. Larsen, and P. Roepstorff. 1998. Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: strategies and applications. Proteins. Suppl. 2:74-89.
    • (1998) Proteins. Suppl. , vol.2 , pp. 74-89
    • Jensen, O.N.1    Larsen, M.R.2    Roepstorff, P.3
  • 26
    • 0032476605 scopus 로고    scopus 로고
    • Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex
    • Katz, L., P.I. Hanson, J.E. Heuser, and P. Brennwald. 1998. Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex. EMBO (Eur. Mol. Biol. Org.) J. 17:6200-6209.
    • (1998) EMBO (Eur. Mol. Biol. Org.) J. , vol.17 , pp. 6200-6209
    • Katz, L.1    Hanson, P.I.2    Heuser, J.E.3    Brennwald, P.4
  • 28
    • 0030668326 scopus 로고    scopus 로고
    • Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic
    • Lupashin, V.V., I.D. Pokrovskaya, J.A. McNew, and M.G. Waters. 1997. Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic. Mol. Biol. Cell 8:2659-2676.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2659-2676
    • Lupashin, V.V.1    Pokrovskaya, I.D.2    McNew, J.A.3    Waters, M.G.4
  • 29
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) precedes docking and fusion of yeast vacuoles
    • Mayer, A., W. Wickner, and A. Haas. 1996. Sec18p (NSF)-driven release of Sec17p (α-SNAP) precedes docking and fusion of yeast vacuoles. Cell. 85: 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 31
    • 0032537835 scopus 로고    scopus 로고
    • Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes
    • Mills, I.G., A.T. Jones, and M.J. Clague. 1998. Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes. Curr. Biol. 8:881-884.
    • (1998) Curr. Biol. , vol.8 , pp. 881-884
    • Mills, I.G.1    Jones, A.T.2    Clague, M.J.3
  • 33
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of rab proteins in vesicle transport
    • Novick, P., and M. Zerial. 1997. The diversity of rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9:496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 34
    • 0030954439 scopus 로고    scopus 로고
    • Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin and SNAP-25 in the membrane of synaptic vesicles
    • Otto, H., P.I. Hanson, and R. Jahn. 1997. Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin and SNAP-25 in the membrane of synaptic vesicles. Proc. Natl. Acad. Sci. USA. 94:6197-6201.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6197-6201
    • Otto, H.1    Hanson, P.I.2    Jahn, R.3
  • 35
    • 0032506349 scopus 로고    scopus 로고
    • Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • Peters, C., and A. Mayer. 1998. Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature. 396:575-580.
    • (1998) Nature , vol.396 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 36
    • 0029752048 scopus 로고    scopus 로고
    • Transport vesicle docking: SNARE and associates
    • Pfeffer, S.R. 1996. Transport vesicle docking: SNARE and associates. Annu. Rev. Cell Biol. Dev. Biol. 12:441-461.
    • (1996) Annu. Rev. Cell Biol. Dev. Biol. , vol.12 , pp. 441-461
    • Pfeffer, S.R.1
  • 37
    • 0030852699 scopus 로고    scopus 로고
    • The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway
    • Piper, R.C., N.J. Bryant, and T.H. Stevens. 1997. The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. J. Cell Biol. 138:531-545.
    • (1997) J. Cell Biol. , vol.138 , pp. 531-545
    • Piper, R.C.1    Bryant, N.J.2    Stevens, T.H.3
  • 39
    • 0028143698 scopus 로고
    • Mechanisms of intracellular membrane fusion
    • Rothman, J.E. 1994. Mechanisms of intracellular membrane fusion. Nature. 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 40
    • 0032584707 scopus 로고    scopus 로고
    • Functional reconstitution of Ypt7p GTPase and a purified vacuole SNARE complex
    • Sato, K., and W. Wickner. 1998. Functional reconstitution of Ypt7p GTPase and a purified vacuole SNARE complex. Science. 281:700-702.
    • (1998) Science , vol.281 , pp. 700-702
    • Sato, K.1    Wickner, W.2
  • 41
    • 0031841313 scopus 로고    scopus 로고
    • Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking
    • Sato, K., T. Darsow, and S.E. Emr. 1998. Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Mol. Cell Biol. 18:5308-5319.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5308-5319
    • Sato, K.1    Darsow, T.2    Emr, S.E.3
  • 42
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 46
    • 0032476574 scopus 로고    scopus 로고
    • Reconstitution of retrograde transport from the Golgi to the ER in vitro
    • Spang, A., and R. Scheckman. 1998. Reconstitution of retrograde transport from the Golgi to the ER in vitro. J. Cell Biol. 143:589-599.
    • (1998) J. Cell Biol. , vol.143 , pp. 589-599
    • Spang, A.1    Scheckman, R.2
  • 47
    • 0031932616 scopus 로고    scopus 로고
    • Pth1/Vam3p is the syntaxin homolog at the vacuolar membrane of Saccharomyces cerevisiae required for the delivery of vacuolar hydrolases
    • Srivastava, A., and E.W. Jones. 1998. Pth1/Vam3p is the syntaxin homolog at the vacuolar membrane of Saccharomyces cerevisiae required for the delivery of vacuolar hydrolases. Genetics. 148:85-98.
    • (1998) Genetics , vol.148 , pp. 85-98
    • Srivastava, A.1    Jones, E.W.2
  • 48
    • 0033555524 scopus 로고    scopus 로고
    • A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G protein-coupled receptor
    • Stefan, C.J., and K.J. Blumer. 1999. A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G protein-coupled receptor. J. Biol. Chem. 274:1835-1841.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1835-1841
    • Stefan, C.J.1    Blumer, K.J.2
  • 49
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
    • Stenmark, H., G. Vitale, O. Ullrich, and M. Zerial. 1995. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell. 83: 423-432.
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 50
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R.B., D. Fasshauer, R. Jahn, and A.T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 51
    • 0031847684 scopus 로고    scopus 로고
    • Formation and turnover of NSF-and SNAP-containing "fusion" complexes occurs on undocked, clathrin-coated vesicle-derived membranes
    • Swanton, E., J. Sheehan, N. Bishop, S. High, and P. Woodman. 1998. Formation and turnover of NSF-and SNAP-containing "fusion" complexes occurs on undocked, clathrin-coated vesicle-derived membranes. Mol. Biol. Cell. 9:1633-1637.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1633-1637
    • Swanton, E.1    Sheehan, J.2    Bishop, N.3    High, S.4    Woodman, P.5
  • 52
    • 0032509210 scopus 로고    scopus 로고
    • Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion
    • Tahara, M., J. Coorssen, K. Timmers, P.S. Blank, T. Whalley, R. Scheller, and J. Zimmerberg. 1998. Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion. J. Biol. Chem. 273:33667-33673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33667-33673
    • Tahara, M.1    Coorssen, J.2    Timmers, K.3    Blank, P.S.4    Whalley, T.5    Scheller, R.6    Zimmerberg, J.7
  • 53
    • 0032526955 scopus 로고    scopus 로고
    • Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion
    • Ungermann, C., and W. Wickner. 1998. Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. EMBO (Eur. Mol. Biol. Org.) J. 17:3269-3276.
    • (1998) EMBO (Eur. Mol. Biol. Org.) J. , vol.17 , pp. 3269-3276
    • Ungermann, C.1    Wickner, W.2
  • 54
    • 0031942615 scopus 로고    scopus 로고
    • A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated organelles, is disassembled and activated for docking and fusion
    • Ungermann, C., B.J. Nichols, H.R.B. Pelham, and W. Wickner. 1998a. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated organelles, is disassembled and activated for docking and fusion. J. Cell Biol. 140:61-69.
    • (1998) J. Cell Biol. , vol.140 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.B.3    Wickner, W.4
  • 55
    • 0032506543 scopus 로고    scopus 로고
    • Defining the function of trans SNARE pairs
    • Ungermann, C., K. Sato, and W. Wickner. 1998b. Defining the function of trans SNARE pairs. Nature. 396:543-548.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 56
    • 0030968166 scopus 로고    scopus 로고
    • Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae
    • Wada, Y., N. Nakamura, Y. Ohsumi, and A. Hirata. 1997. Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae. J. Cell Sci. 110:1299-1306.
    • (1997) J. Cell Sci. , vol.110 , pp. 1299-1306
    • Wada, Y.1    Nakamura, N.2    Ohsumi, Y.3    Hirata, A.4
  • 57
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
    • Walch-Solimena, C., J. Blasi, L. Edelmann, L., E.R. Chapman, G. Fischer von Mollard, and R. Jahn. 1995. The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. J. Cell Biol. 128:637-645.
    • (1995) J. Cell Biol. , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.L.3    Chapman, E.R.4    Von Mollard, G.F.5    Jahn, R.6
  • 59
    • 12644298688 scopus 로고    scopus 로고
    • A conserved domain is present in different families of vesicular fusion proteins: A new superfamily
    • Weimbs, T., S.H. Low, S.J. Chapin, K.E. Mostov, P. Bucher, and K. Hofmann. 1997. A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Proc. Natl. Acad. Sci. USA. 94:3046-3051.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3046-3051
    • Weimbs, T.1    Low, S.H.2    Chapin, S.J.3    Mostov, K.E.4    Bucher, P.5    Hofmann, K.6
  • 60
    • 0032563766 scopus 로고    scopus 로고
    • Membrane fusion. SNARE the rod, coil the complex
    • Weis, W.I., and R.H. Scheller. 1998. Membrane fusion. SNARE the rod, coil the complex. Nature. 395:328-329.
    • (1998) Nature , vol.395 , pp. 328-329
    • Weis, W.I.1    Scheller, R.H.2
  • 61
    • 0029981513 scopus 로고    scopus 로고
    • Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae
    • Xu, Z., and W. Wickner. 1996. Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae. J. Cell Biol. 132:787-794.
    • (1996) J. Cell Biol. , vol.132 , pp. 787-794
    • Xu, Z.1    Wickner, W.2
  • 62
    • 0032568798 scopus 로고    scopus 로고
    • LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion
    • Xu, Z., K. Sato, and W. Wickner. 1998. LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell. 93:1125-1134.
    • (1998) Cell , vol.93 , pp. 1125-1134
    • Xu, Z.1    Sato, K.2    Wickner, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.