메뉴 건너뛰기




Volumn 17, Issue 12, 1998, Pages 3269-3276

Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion

Author keywords

SNAP 25; SNARE complex; Vacuole fusion; Vam7p

Indexed keywords

CELL MEMBRANE PROTEIN; MUTANT PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 0032526955     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.12.3269     Document Type: Article
Times cited : (98)

References (60)
  • 4
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25 like component of the yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald, P., Kearns, B., Champion, K., Keränen, S., Bankaitis, V. and Novick, P. (1994) Sec9 is a SNAP-25 like component of the yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell, 79, 245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keränen, S.4    Bankaitis, V.5    Novick, P.6
  • 5
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., Ballew, N. and Barlowe, C. (1998) Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J., 17, 2156-2165.
    • (1998) EMBO J. , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 6
    • 0027973132 scopus 로고
    • SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils
    • Chapman, E.R., An, S., Barton, N. and Jahn, R. (1994) SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. J. Biol. Chem., 269, 27427-27432.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27427-27432
    • Chapman, E.R.1    An, S.2    Barton, N.3    Jahn, R.4
  • 7
    • 0027093271 scopus 로고
    • In vitro reactions of vacuole inheritance in Saccharomyces cerevisiae
    • Conradt, B., Shaw, J., Vida, T., Emr, S. and Wickner, W. (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.4    Wickner, W.5
  • 8
    • 0027992040 scopus 로고
    • Yeast Snc proteins complex with Sec9
    • Couves, A. and Gerst, J.E. (1994) Yeast Snc proteins complex with Sec9. J. Biol. Chem., 269, 23391-23394.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23391-23394
    • Couves, A.1    Gerst, J.E.2
  • 9
    • 0031041456 scopus 로고    scopus 로고
    • A structural change occurs upon binding of syntaxin to SNAP-25
    • Fasshauer, D., Bruns, D., Shen, B., Jahn, R. and Brünger, A.T. (1997a) A structural change occurs upon binding of syntaxin to SNAP-25. J. Biol. Chem., 272, 4582-4590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4582-4590
    • Fasshauer, D.1    Bruns, D.2    Shen, B.3    Jahn, R.4    Brünger, A.T.5
  • 10
    • 0030735370 scopus 로고    scopus 로고
    • Structural changes are associated with soluble N-ethylmleimide-sensitive fusion protein attachment protein receptor complex formation
    • Fasshauer, D., Henning, O., Eliason, W.K., Jahn, R. and Brünger, A.T. (1997b) Structural changes are associated with soluble N-ethylmleimide-sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem., 272, 28036-28041.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Henning, O.2    Eliason, W.K.3    Jahn, R.4    Brünger, A.T.5
  • 11
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick, S. and Jahn, R. (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
    • 0030990122 scopus 로고    scopus 로고
    • The yeast v-SNARE Vtilp mediates two vesicle transport pathways through interaction with the t-SNAREs Sed5p and Pep12p
    • Fischer von Mollard, G., Notwehr, S. and Stevens, T. (1997) The yeast v-SNARE Vtilp mediates two vesicle transport pathways through interaction 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.3
  • 14
    • 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. Methods Cell Sci., 17, 283-294.
    • (1995) Methods Cell Sci. , vol.17 , pp. 283-294
    • Haas, A.1
  • 15
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuolar fusion requires Sec17p (yeast α-SNAP) and Sec18p (yeast NSF)
    • Haas, A. and Wickner, W. (1996) Homotypic vacuolar fusion requires Sec17p (yeast α-SNAP) and Sec18p (yeast NSF). EMBO J., 15, 3296-3305.
    • (1996) EMBO J. , vol.15 , pp. 3296-3305
    • Haas, A.1    Wickner, W.2
  • 16
    • 0028333056 scopus 로고
    • G-protein ligands inhibit in vitro reactions of vacuole inheritance
    • Haas, A., Conradt, B. and Wickner, W. (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
  • 17
    • 0028788311 scopus 로고
    • The GTPase Ypt7p is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance
    • Haas, A., Scheglmann, D., Lazar, T., Gallwitz, D. and Wickner, W. (1995) The GTPase Ypt7p is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance. EMBO J., 14, 5258-5270.
    • (1995) EMBO J. , vol.14 , pp. 5258-5270
    • Haas, A.1    Scheglmann, D.2    Lazar, T.3    Gallwitz, D.4    Wickner, W.5
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • Harlow, E. and Lane, O. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, O.2
  • 19
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C.A. and Südhof, T.C. (1993) Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature. 366, 347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 20
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion Curr
    • Hay, J.C. and Scheller, R. (1997) SNAREs and NSF in targeted membrane fusion Curr. Opin. Cell Biol., 9, 505-512.
    • (1997) Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.2
  • 21
    • 0030890594 scopus 로고    scopus 로고
    • Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Hay, J.C., Chao, D.S., Kuo, C. and Scheller, R.H. (1997) Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Cell, 89, 149-158.
    • (1997) Cell , vol.89 , pp. 149-158
    • Hay, J.C.1    Chao, D.S.2    Kuo, C.3    Scheller, R.H.4
  • 22
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Südhof, T.C. and Niemann, H. (1994) Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J., 13, 5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 23
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi, T., Yamasaki, S., Nauenburg, S., Binz, T. and Niemann, H. (1995) Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J., 14, 2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 24
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system in yeast
    • Holthuis, J.C.M., Nichols, B.J., Dhruvakumar, S. and Pelham, H.R.B. (1998) Two syntaxin homologues in the TGN/endosomal system in yeast. EMBO J., 17, 113-126.
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.C.M.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.B.4
  • 25
    • 0027241227 scopus 로고
    • Bos1p, an integral membrane protein of the ER to Golgi transport vesicle, is required for their fusion competence
    • Lian, J.P. and Ferro-Novick, S. (1993) Bos1p, an integral membrane protein of the ER to Golgi transport vesicle, is required for their fusion competence. Cell, 73, 735-745.
    • (1993) Cell , vol.73 , pp. 735-745
    • Lian, J.P.1    Ferro-Novick, S.2
  • 26
    • 0031001794 scopus 로고    scopus 로고
    • t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase
    • Lupashin, V.V. and Waters, M.G. (1997) t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase. Science, 276, 1255-1258.
    • (1997) Science , vol.276 , pp. 1255-1258
    • Lupashin, V.V.1    Waters, M.G.2
  • 27
    • 0030668326 scopus 로고    scopus 로고
    • Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic
    • Lupashin, V.V., Pokrovskaya, I.D., McNew, J.A., Waters, M.G. (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
  • 28
    • 0030857288 scopus 로고    scopus 로고
    • Stages of regulated exocytosis
    • Martin, T.F.J. (1997) Stages of regulated exocytosis. Trends Cell Biol., 7, 271-276.
    • (1997) Trends Cell Biol. , vol.7 , pp. 271-276
    • Martin, T.F.J.1
  • 29
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer, A. and Wickner, W. (1997) Docking of yeast vacuoles is catalyzed by the ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol., 136, 307-317.
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 30
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) precedes docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W. and Haas, A. (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
    • 0028963427 scopus 로고
    • Synaptic core complex of synaptobrevin, syntaxin, and SNAP-25 forms high affinity alpha- SNAP binding site
    • McMahon, H.T. and Sudhof, T.C. (1995) Synaptic core complex of synaptobrevin, syntaxin, and SNAP-25 forms high affinity alpha-SNAP binding site. J. Biol. Chem., 270, 2213-2217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2213-2217
    • McMahon, H.T.1    Sudhof, T.C.2
  • 33
    • 0031940772 scopus 로고    scopus 로고
    • Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast
    • Neiman, A.M. (1998) Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast. J. Cell Biol., 140, 29-37.
    • (1998) J. Cell Biol. , vol.140 , pp. 29-37
    • Neiman, A.M.1
  • 34
    • 0026705918 scopus 로고
    • Bos1p, a membrane protein required for ER to Golgi transport in yeast, co- Purifies with the carrier vesicles and with Bet1p and the ER membrane
    • Newman, A.P. Groesch, M. and Ferro-Novick, S. (1992) Bos1p, a membrane protein required for ER to Golgi transport in yeast, co-purifies with the carrier vesicles and with Bet1p and the ER membrane. EMBO J., 12, 3609-3617.
    • (1992) EMBO J. , vol.12 , pp. 3609-3617
    • Newman, A.P.1    Groesch, M.2    Ferro-Novick, S.3
  • 36
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of rab proteins in vesicle transport
    • Novick, P. and Zerial, M. (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
  • 37
    • 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., Hanson, P.I. and Jahn, R. (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
  • 39
    • 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
  • 40
    • 0030761156 scopus 로고    scopus 로고
    • Formation of a yeast SNARE complex is accompanied by significant structural changes
    • Rice, L.M., Brennwald, P. and Brünger, A.T. (1997) Formation of a yeast SNARE complex is accompanied by significant structural changes. FEBS Lett., 415, 49-55.
    • (1997) FEBS Lett. , vol.415 , pp. 49-55
    • Rice, L.M.1    Brennwald, P.2    Brünger, A.T.3
  • 41
    • 0030952226 scopus 로고    scopus 로고
    • Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog. Sec9
    • Rossi, G., Salminen, A., Rice, L.M., Brünger, A.T. and Brennwald, P. (1997) Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog. Sec9. J. Biol. Chem., 272, 16610-16617.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16610-16617
    • Rossi, G.1    Salminen, A.2    Rice, L.M.3    Brünger, A.T.4    Brennwald, P.5
  • 42
    • 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
  • 43
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Søgaard, M., Tani, K., Ye, R.R., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, J.E. and Söllner, T. (1994) A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell, 78, 937-48.
    • (1994) Cell , vol.78 , pp. 937-948
    • Søgaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Söllner, T.8
  • 45
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion
    • Söllner, T., Bennett, M.K., Whiteheart, S., Scheller, R.H. and Rothman, J.E. (1993b) A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion. Cell, 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.3    Scheller, R.H.4    Rothman, J.E.5
  • 47
    • 0029026392 scopus 로고
    • The synaptic vesicle cascade: A cascade of protein-protein interactions
    • Südhof, T.C. (1995) The synaptic vesicle cascade: a cascade of protein-protein interactions. Nature, 342, 645-653.
    • (1995) Nature , vol.342 , pp. 645-653
    • Südhof, T.C.1
  • 49
    • 0030599203 scopus 로고    scopus 로고
    • SNAP-25 is present on chromaffin granules and acts as a SNAP receptor
    • Tagaya, M., Genma, T., Yamamoto, A., Kozaki, S. and Mizushima, S. (1996) SNAP-25 is present on chromaffin granules and acts as a SNAP receptor. FEBS Lett., 394, 83-86.
    • (1996) FEBS Lett. , vol.394 , pp. 83-86
    • Tagaya, M.1    Genma, T.2    Yamamoto, A.3    Kozaki, S.4    Mizushima, S.5
  • 50
    • 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., Nichols, B.J., Pelham, H.R.B. and Wickner, W. (1998) 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
  • 51
    • 18244432240 scopus 로고    scopus 로고
    • Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
    • Veit, M., Söllner, T.H. and Rothman, J.E. (1996) Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25. FEBS Lett., 385, 119-123.
    • (1996) FEBS Lett. , vol.385 , pp. 119-123
    • Veit, M.1    Söllner, T.H.2    Rothman, J.E.3
  • 52
    • 0026668576 scopus 로고
    • Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. VAM7, a gene for regulating morphogenic assembly of the vacuoles
    • Wada, Y. and Anraku, Y. (1992) Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. VAM7, a gene for regulating morphogenic assembly of the vacuoles. J. Biol. Chem., 267, 18671-18675.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18671-18675
    • Wada, Y.1    Anraku, Y.2
  • 53
    • 0026629819 scopus 로고
    • Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. Isolation and characterization of two classes of vam mutants
    • Wada, Y. Ohsumi, Y. and Anraku, Y. (1992) Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. Isolation and characterization of two classes of vam mutants. J. Biol. Chem., 267, 18665-18670.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18665-18670
    • Wada, Y.1    Ohsumi, Y.2    Anraku, Y.3
  • 54
    • 0030968166 scopus 로고    scopus 로고
    • Vam3p, a new member of syntaxin related proteins, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae
    • Wada, Y. Nakamura, N., Ohsumi, Y. and Hirata, A. (1997) Vam3p, a new member of syntaxin related proteins, 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
  • 55
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
    • Walch-Solimena, C., Blasi, J., Edelmann, L., Chapman, E.R., Fischer von Mollard, G. and Jahn, R. (1995) The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. J. Cell Biol., 128, 637-45.
    • (1995) J. Cell Biol. , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.3    Chapman, E.R.4    Fischer Von Mollard, G.5    Jahn, R.6
  • 56
    • 12644298688 scopus 로고    scopus 로고
    • A conserved domain is present in different families of vesicular fusion proteins: A new superfamily
    • Weimbs, T., Low, S.H., Chapin, S.J., Mostov, K.E., Bucher, P. and Hofmann, K. (1997) A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Proc. Natl Acad. Sci., 94, 3046-3051.
    • (1997) Proc. Natl Acad. Sci. , 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
  • 57
    • 0029981513 scopus 로고    scopus 로고
    • Thioredoxin is required for vacuole inheritance in S.cerevisiae
    • Xu, Z. and Wickner, W. (1996) Thioredoxin is required for vacuole inheritance in S.cerevisiae. J. Cell Biol., 132, 787-794.
    • (1996) J. Cell Biol. , vol.132 , pp. 787-794
    • Xu, Z.1    Wickner, W.2
  • 58
    • 0031047480 scopus 로고    scopus 로고
    • 2 cooperates with Sec18p(NSF) to promote yeast vacuole inheritance
    • 2 cooperates with Sec18p(NSF) to promote yeast vacuole inheritance. J. Cell Biol., 136, 299-306.
    • (1997) J. Cell Biol. , vol.136 , pp. 299-306
    • Xu, Z.1    Mayer, A.2    Muller, E.3    Wickner, W.4
  • 59
    • 0345284209 scopus 로고    scopus 로고
    • LMA1 binds to vacuoles via Sec18p (NSF), transfers after ATP-hydrolysis to a complex with the t-SNARE (Vam3p), and is released during organelle fusion
    • in press
    • Xu, Z., Sato, K. and Wickner, W. (1998) LMA1 binds to vacuoles via Sec18p (NSF), transfers after ATP-hydrolysis to a complex with the t-SNARE (Vam3p), and is released during organelle fusion. Cell, in press.
    • (1998) Cell
    • Xu, Z.1    Sato, K.2    Wickner, W.3
  • 60
    • 1842335138 scopus 로고    scopus 로고
    • The mammalian protein (rbet1) homologous to yeast Betlp is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus
    • Zhang, T., Wong, S.H., Tang, B.L., Xu, Y. Peter, F., Subramaniam, N. and Hong, W. (1997) The mammalian protein (rbet1) homologous to yeast Betlp is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol., 139, 1157-1168.
    • (1997) J. Cell Biol. , vol.139 , pp. 1157-1168
    • Zhang, T.1    Wong, S.H.2    Tang, B.L.3    Xu, Y.4    Peter, F.5    Subramaniam, N.6    Hong, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.