메뉴 건너뛰기




Volumn 15, Issue 13, 1996, Pages 3296-3305

Homotypic vacuole fusion requires sec17p (yeast α-SNAP) and sec18p (yeast NSF)

Author keywords

Membrane fusion; NSF; Organelle inheritance; SNAP; Vacuole

Indexed keywords

ACYL COENZYME A; ANTIBODY; FUNGAL PROTEIN; N ETHYLMALEIMIDE; RECOMBINANT PROTEIN;

EID: 0030015868     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00694.x     Document Type: Article
Times cited : (156)

References (67)
  • 1
    • 0028960491 scopus 로고
    • Reconstitution of vesiculated Golgi membranes into stacks of cisternae: Requirement of NSF in stack formation
    • Acharya, U., McCaffery, J.M., Jacobs, R. and Malhotra, V. (1995a) Reconstitution of vesiculated Golgi membranes into stacks of cisternae: requirement of NSF in stack formation. J. Cell Biol., 129, 577-589.
    • (1995) J. Cell Biol. , vol.129 , pp. 577-589
    • Acharya, U.1    McCaffery, J.M.2    Jacobs, R.3    Malhotra, V.4
  • 2
    • 0029084786 scopus 로고
    • The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events
    • Acharya, U., Jacobs, R., Peters, J.-M., Watson, N., Farquhar, M.G. and Malhotra, V. (1995b) The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events. Cell, 82, 895-904.
    • (1995) Cell , vol.82 , pp. 895-904
    • Acharya, U.1    Jacobs, R.2    Peters, J.-M.3    Watson, N.4    Farquhar, M.G.5    Malhotra, V.6
  • 3
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
    • Balch, W.E., Dunphy, W.G., Braell, W.A. and Rothman, J.E. (1984) Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell, 39, 405-416.
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.E.1    Dunphy, W.G.2    Braell, W.A.3    Rothman, J.E.4
  • 4
    • 0000272957 scopus 로고
    • Isolation of yeast mutants defective in protein targeting to the vacuole
    • Bankaitis, V., Johnson, L.M. and Emr, S.D. (1986) Isolation of yeast mutants defective in protein targeting to the vacuole. Proc. Natl Acad. Sci. USA, 83, 9075-9079.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 9075-9079
    • Bankaitis, V.1    Johnson, L.M.2    Emr, S.D.3
  • 5
    • 0024366928 scopus 로고
    • Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein
    • Beckers, C.J.M., Block. M.R., Glick, B.S., Rothman, J.E. and Balch, W.E. (1989) Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein. Nature, 339, 397-398.
    • (1989) Nature , vol.339 , pp. 397-398
    • Beckers, C.J.M.1    Block, M.R.2    Glick, B.S.3    Rothman, J.E.4    Balch, W.E.5
  • 7
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary, D.O., Griff, I.C. and Rothman, J.E. (1990) SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell, 61, 709-721.
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 8
    • 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
  • 9
    • 0028225582 scopus 로고
    • Determination of four biochemically distinct, sequential stages during vacuole inheritance in vitro
    • Conradt, B., Haas, A. and Wickner, W. (1994) Determination of four biochemically distinct, sequential stages during vacuole inheritance in vitro. J. Cell Biol., 126, 99-110.
    • (1994) J. Cell Biol. , vol.126 , pp. 99-110
    • Conradt, B.1    Haas, A.2    Wickner, W.3
  • 10
    • 0029042360 scopus 로고
    • Yeast synaptobrevin homologs are modified post-translationally by the addition of palmitate
    • Couve, A., Protopopov, V. and Gerst, J.E. (1995) Yeast synaptobrevin homologs are modified post-translationally by the addition of palmitate. Proc. Natl Acad. Sci. USA, 92, 5987-5991.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5987-5991
    • Couve, A.1    Protopopov, V.2    Gerst, J.E.3
  • 11
    • 0024385937 scopus 로고
    • Vesicle fusion following receptor-mediated endocytosis requires a protein active in Golgi transport
    • Diaz, R., Mayorga, L.S., Weidman, P.J., Rothman, J.E. and Stahl, P.D. (1989) Vesicle fusion following receptor-mediated endocytosis requires a protein active in Golgi transport. Nature, 339, 398-400.
    • (1989) Nature , vol.339 , pp. 398-400
    • Diaz, R.1    Mayorga, L.S.2    Weidman, P.J.3    Rothman, J.E.4    Stahl, P.D.5
  • 12
    • 0024094923 scopus 로고
    • Characterization of a component of the yeast secretory machinery: Identification of the SEC18 gene product
    • Eakle, K.A., Bernstein, M. and Emr, S.D. (1988) Characterization of a component of the yeast secretory machinery: Identification of the SEC18 gene product. Mol. Cell. Biol., 8, 4098-4109.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4098-4109
    • Eakle, K.A.1    Bernstein, M.2    Emr, S.D.3
  • 13
    • 0024389333 scopus 로고
    • Structure and function of vacuolar class of ATP-driven proton pumps
    • Forgac, M. (1989) Structure and function of vacuolar class of ATP-driven proton pumps. Physiol. Rev., 69, 765-795.
    • (1989) Physiol. Rev. , vol.69 , pp. 765-795
    • Forgac, M.1
  • 14
    • 0025913947 scopus 로고
    • Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation and gene expression
    • Fröhlich, K.-U., Fries, H.-W., Rüdiger, M., Erdmann, R., Botstein, D. and Mecker, D. (1991) Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation and gene expression. J. Cell Biol., 114, 443-453.
    • (1991) J. Cell Biol. , vol.114 , pp. 443-453
    • Fröhlich, K.-U.1    Fries, H.-W.2    Rüdiger, M.3    Erdmann, R.4    Botstein, D.5    Mecker, D.6
  • 15
    • 0023091173 scopus 로고
    • Possible role for fatty acyl-coenzyme a in intracellular protein transport
    • Glick, B.S. and Rothman, J.E. (1987) Possible role for fatty acyl-coenzyme A in intracellular protein transport. Nature, 326, 309-312.
    • (1987) Nature , vol.326 , pp. 309-312
    • Glick, B.S.1    Rothman, J.E.2
  • 16
    • 0026061021 scopus 로고
    • Identification of a novel, N-ethylmaleimide-sensitive cytosolic factor required for vesicular transport from endosomes to the trans-Golgi network in vitro
    • Goda, Y. and Pfeffer, S.R. (1991) Identification of a novel, N-ethylmaleimide-sensitive cytosolic factor required for vesicular transport from endosomes to the trans-Golgi network in vitro. J. Cell Biol., 112, 823-831.
    • (1991) J. Cell Biol. , vol.112 , pp. 823-831
    • Goda, Y.1    Pfeffer, S.R.2
  • 17
    • 0025952205 scopus 로고
    • Vacuolar segregation to the bud of Saccharomyces cerevisiae: An analysis of morphology and timing in the cell cycle
    • Gomes de Mesquita, D.S., ten Hoopen, R. and Woldringh, C.L. (1991) Vacuolar segregation to the bud of Saccharomyces cerevisiae: an analysis of morphology and timing in the cell cycle. J. Gen. Microbiol., 137, 2447-2454.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2447-2454
    • Gomes De Mesquita, D.S.1    Ten Hoopen, R.2    Woldringh, C.L.3
  • 18
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T.R. and Emr, S.D. (1991) Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol., 114, 207-218.
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 19
    • 0026692898 scopus 로고
    • The yeast SEC17 gene product is functionally equivalent to mammalian α-SNAP protein
    • Griff, I.C., Schekman, R., Rothman, J.E. and Kaiser, C.A. (1992) The yeast SEC17 gene product is functionally equivalent to mammalian α-SNAP protein. J. Biol. Chem., 267, 12106-12115.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12106-12115
    • Griff, I.C.1    Schekman, R.2    Rothman, J.E.3    Kaiser, C.A.4
  • 20
    • 0242610086 scopus 로고    scopus 로고
    • A quantitative assay to measure homotypic vacuole fusion in vitro
    • in press
    • Haas, A. (1996) A quantitative assay to measure homotypic vacuole fusion in vitro. Methods Cell Sci., in press.
    • (1996) Methods Cell Sci.
    • Haas, A.1
  • 21
    • 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
  • 22
    • 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
  • 23
    • 0026471991 scopus 로고
    • The 25kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess, D.T., Slater, T.M., Wislon, M.C. and Skeene, J.H.P. (1992) The 25kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci., 12, 4634-4641.
    • (1992) J. Neurosci. , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wislon, M.C.3    Skeene, J.H.P.4
  • 24
    • 0029062772 scopus 로고
    • Different requirements for NSF-SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., Tagaya, M., Ullrich, O., Montecucco, C. and Simons, K. (1995) Different requirements for NSF-SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell, 81, 571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 25
    • 0027194161 scopus 로고
    • Video microscopy of organelle inheritance and mobility in budding yeast
    • Jones, H.D., Schliwa, M. and Drubin, D.G. (1993) Video microscopy of organelle inheritance and mobility in budding yeast. Cell Motil. Cytoskel., 25, 129-142.
    • (1993) Cell Motil. Cytoskel. , vol.25 , pp. 129-142
    • Jones, H.D.1    Schliwa, M.2    Drubin, D.G.3
  • 26
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
    • Kaiser, C.A. and Schekman, R. (1990) Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell. 61, 723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.A.1    Schekman, R.2
  • 27
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky, D.J., Herman, P.K. and Emr, S.D. (1990) The fungal vacuole: composition, function, and biogenesis. Microbiol. Rev., 54, 266-292.
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 28
    • 0022467016 scopus 로고
    • Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids
    • Lambrecht, B. and Schmidt, M.F.G. (1986) Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids. FEBS Lett., 202, 127-132.
    • (1986) FEBS Lett. , vol.202 , pp. 127-132
    • Lambrecht, B.1    Schmidt, M.F.G.2
  • 29
    • 0028365624 scopus 로고
    • The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion
    • Latterich, M. and Schekman, R. (1994) The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion. Cell, 78, 87-98.
    • (1994) Cell , vol.78 , pp. 87-98
    • Latterich, M.1    Schekman, R.2
  • 30
    • 0028365624 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Fröhlich, K.-U. and Schekman, R. (1994) Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell, 78, 87-98.
    • (1994) Cell , vol.78 , pp. 87-98
    • Latterich, M.1    Fröhlich, K.-U.2    Schekman, R.3
  • 31
    • 0023707176 scopus 로고
    • Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack
    • Malhotra, V., Orci, L., Glick, B.S., Block, M.R. and Rothman, J.E. (1988) Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack. Cell. 54, 221-227.
    • (1988) Cell , vol.54 , pp. 221-227
    • Malhotra, V.1    Orci, L.2    Glick, B.S.3    Block, M.R.4    Rothman, J.E.5
  • 32
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W. and Haas, A. (1996) Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede 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
  • 33
    • 0029129193 scopus 로고
    • Enigma variations: Protein mediators of membrane fusion
    • Mellman, I. (1995) Enigma variations: protein mediators of membrane fusion. Cell, 82, 869-872.
    • (1995) Cell , vol.82 , pp. 869-872
    • Mellman, I.1
  • 34
    • 0023091482 scopus 로고
    • Protease B of Saccharomyces cerevisiae: Isolation and regulation of the PRBI structural gene
    • Moehle, C.M., Ayanardi, M.W., Kolodny, M.R., Park, F.J. and Jones, E.W. (1986) Protease B of Saccharomyces cerevisiae: isolation and regulation of the PRBI structural gene. Genetics, 115, 255-263.
    • (1986) Genetics , vol.115 , pp. 255-263
    • Moehle, C.M.1    Ayanardi, M.W.2    Kolodny, M.R.3    Park, F.J.4    Jones, E.W.5
  • 36
    • 0028149757 scopus 로고
    • The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins
    • Morgan, A., Dimaline, R. and Burgoyne, R.D. (1994) The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins. J. Biol. Chem., 269, 29347-29350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29347-29350
    • Morgan, A.1    Dimaline, R.2    Burgoyne, R.D.3
  • 37
    • 0040737237 scopus 로고
    • Protein palmitoylation in membrane trafficking
    • Mundy, D.I. (1995) Protein palmitoylation in membrane trafficking. Biochem. Soc. Trans., 116, 135-146.
    • (1995) Biochem. Soc. Trans. , vol.116 , pp. 135-146
    • Mundy, D.I.1
  • 38
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve, C.W. and Williams, D. (1990) Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J., 9, 3857-3866.
    • (1990) EMBO J. , vol.9 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 39
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C. and Schekman, R. (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell, 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 40
    • 0028239912 scopus 로고
    • GTPases: Multifunctional molecular switches regulating vesicular traffic
    • Nuoffer, C. and Balch, W.E. (1994) GTPases: multifunctional molecular switches regulating vesicular traffic. Annu. Rev. Biochem., 63, 949-990.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 949-990
    • Nuoffer, C.1    Balch, W.E.2
  • 42
    • 0025249975 scopus 로고
    • Fatty acylation promotes fusion of transport vesicles with Golgi cisternae
    • Pfanner, N., Glick, B.S., Arden, S.R. and Rothman, J.E. (1990) Fatty acylation promotes fusion of transport vesicles with Golgi cisternae. J. Cell Biol., 110, 955-961.
    • (1990) J. Cell Biol. , vol.110 , pp. 955-961
    • Pfanner, N.1    Glick, B.S.2    Arden, S.R.3    Rothman, J.E.4
  • 43
    • 0024435355 scopus 로고
    • Fatty acyl-coenzyme a is required for budding of transport vesicles from Golgi cisternae
    • Pfanner, N., Orci, L., Glick, B.S., Amherdt, M., Arden, S.R., Malhotra, V., and Rothman, J.E. (1989) Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae. Cell, 59, 95-102.
    • (1989) Cell , vol.59 , pp. 95-102
    • Pfanner, N.1    Orci, L.2    Glick, B.S.3    Amherdt, M.4    Arden, S.R.5    Malhotra, V.6    Rothman, J.E.7
  • 44
    • 0028033931 scopus 로고
    • Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface
    • Quesnel, S. and Silvius, J.R. (1994) Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface. Biochemistry, 33, 13340-13348.
    • (1994) Biochemistry , vol.33 , pp. 13340-13348
    • Quesnel, S.1    Silvius, J.R.2
  • 45
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate asternal regrowth from mitotic Golgi fragments
    • Rabouille, C., Levine, T.P., Peters, J.-M. and Warren, G. (1995) An NSF-like ATPase, p97, and NSF mediate asternal regrowth from mitotic Golgi fragments. Cell, 82, 905-914.
    • (1995) Cell , vol.82 , pp. 905-914
    • Rabouille, C.1    Levine, T.P.2    Peters, J.-M.3    Warren, G.4
  • 47
    • 0025775567 scopus 로고
    • Distinct biochemical requirements for budding, targeting, and fusion of ER-derived transport vesicles
    • Rexach, M.F. and Schekman, R.W. (1991) Distinct biochemical requirements for budding, targeting, and fusion of ER-derived transport vesicles. J. Cell Biol., 114, 219-229.
    • (1991) J. Cell Biol. , vol.114 , pp. 219-229
    • Rexach, M.F.1    Schekman, R.W.2
  • 48
    • 0028142717 scopus 로고
    • Multiple N-ethylmaleimide-sensitive components are required for endosomal vesicle fusion
    • Rodriguez, L., Stirling, C.J. and Woodman, P.G. (1994) Multiple N-ethylmaleimide-sensitive components are required for endosomal vesicle fusion. Mol. Biol. Cell, 5, 773-783.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 773-783
    • Rodriguez, L.1    Stirling, C.J.2    Woodman, P.G.3
  • 49
    • 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
  • 50
    • 0027449288 scopus 로고
    • Involvement of Ypt7p, a small GTPase, in traffic from late endosomes to the vacuole in yeast
    • Schimmöller, F. and Riezman, H. (1993) Involvement of Ypt7p, a small GTPase, in traffic from late endosomes to the vacuole in yeast. J. Cell Sci., 106, 823-830.
    • (1993) J. Cell Sci. , vol.106 , pp. 823-830
    • Schimmöller, F.1    Riezman, H.2
  • 51
    • 0025806504 scopus 로고
    • Vac2: A yeast mutant which distinguishes vacuole segregation from Golgi-to-vacuole protein targeting
    • Shaw, J. and Wickner, W. (1991) vac2: a yeast mutant which distinguishes vacuole segregation from Golgi-to-vacuole protein targeting. EMBO J., 10, 1741-1748.
    • (1991) EMBO J. , vol.10 , pp. 1741-1748
    • Shaw, J.1    Wickner, W.2
  • 53
    • 0028096570 scopus 로고
    • Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport
    • Sumida, M., Hong, R.-M. and Tagaya, M. (1994) Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport. J. Biol. Chem., 269, 20636-20641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20636-20641
    • Sumida, M.1    Hong, R.-M.2    Tagaya, M.3
  • 54
    • 0027463890 scopus 로고
    • Control of protein traffic between distinct plasma membrane domains
    • Sztul, E., Colombo, M., Stahl, P. and Samanta, R. (1993) Control of protein traffic between distinct plasma membrane domains. J. Biol. Chem., 268, 1876-1885.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1876-1885
    • Sztul, E.1    Colombo, M.2    Stahl, P.3    Samanta, R.4
  • 55
    • 0026629819 scopus 로고
    • Genes for directing vacuoles morphogenesis in Saccharomyces cerevisiae
    • Wada, Y., Ohsumi, Y. and Anraku, Y. (1992) Genes for directing vacuoles morphogenesis in Saccharomyces cerevisiae. J. Biol. Chem., 267, 18665-18670.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18665-18670
    • Wada, Y.1    Ohsumi, Y.2    Anraku, Y.3
  • 56
    • 0026658185 scopus 로고
    • The activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (α-SNAP) during vesicle formation
    • Wattenberg, B.W., Raub, T.J., Hiebsch, R.R. and Weidman, P.J. (1992) The activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (α-SNAP) during vesicle formation. J. Cell Biol., 118, 1321-1332.
    • (1992) J. Cell Biol. , vol.118 , pp. 1321-1332
    • Wattenberg, B.W.1    Raub, T.J.2    Hiebsch, R.R.3    Weidman, P.J.4
  • 57
    • 0024514664 scopus 로고
    • Binding of an N-ethylmaleimide-sensitive fusion protein to Golgi membranes requires both a soluble protein(s) and an integral membrane receptor
    • Weidman, P.J., Melançon, P., Block, M.R. and Rothman, J.E. (1989) Binding of an N-ethylmaleimide-sensitive fusion protein to Golgi membranes requires both a soluble protein(s) and an integral membrane receptor. J. Cell Biol., 108, 1589-1596.
    • (1989) J. Cell Biol. , vol.108 , pp. 1589-1596
    • Weidman, P.J.1    Melançon, P.2    Block, M.R.3    Rothman, J.E.4
  • 58
    • 0024299493 scopus 로고
    • Intervacuole exchange in the yeast zygote: A new pathway in organelle communication
    • Weisman, L.S. and Wickner, W.T. (1988) Intervacuole exchange in the yeast zygote: a new pathway in organelle communication. Science, 241, 289-591.
    • (1988) Science , vol.241 , pp. 289-591
    • Weisman, L.S.1    Wickner, W.T.2
  • 59
    • 0023432180 scopus 로고
    • Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle
    • Weisman, L.S., Bacallao, R. and Wickner, W.T. (1987) Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle. J. Cell Biol., 105, 1539-1547.
    • (1987) J. Cell Biol. , vol.105 , pp. 1539-1547
    • Weisman, L.S.1    Bacallao, R.2    Wickner, W.T.3
  • 60
    • 0025070007 scopus 로고
    • Mutants of Saccharomyces cerevisiae that block intervacuole vesicular traffic and vacuole division and segregation
    • Weisman, L., Emr, S.D. and Wickner, W.T. (1990) Mutants of Saccharomyces cerevisiae that block intervacuole vesicular traffic and vacuole division and segregation. Proc. Natl Acad. Sci. USA, 87, 1076-1080.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1076-1080
    • Weisman, L.1    Emr, S.D.2    Wickner, W.T.3
  • 61
    • 0028835784 scopus 로고
    • SNAPs and NSF: General members of the fusion apparatus
    • Whiteheart, S.W. and Kubalek, E.W. (1995) SNAPs and NSF: general members of the fusion apparatus. Trends Cell Biol., 5, 64-68.
    • (1995) Trends Cell Biol. , vol.5 , pp. 64-68
    • Whiteheart, S.W.1    Kubalek, E.W.2
  • 62
    • 0026720008 scopus 로고
    • Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes
    • Whiteheart, S.W., Brunner, M., Wilson, D.W., Wiedman, M. and Rothman, J.E. (1992) Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes. J. Biol. Chem., 267, 12239-12243.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12239-12243
    • Whiteheart, S.W.1    Brunner, M.2    Wilson, D.W.3    Wiedman, M.4    Rothman, J.E.5
  • 63
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S.W., Rossnagel, K., Buhrow, S.A., Brunner, M., Jaenicke, R. and Rothman, J.E. (1994) N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol., 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 64
    • 0027092937 scopus 로고
    • Endocytosis in yeast: Evidence for the involvement of a small GTP-binding protein (Ypt7p)
    • Wichmann, H., Hengst, L. and Gallwitz, D. (1992) Endocytosis in yeast: evidence for the involvement of a small GTP-binding protein (Ypt7p). Cell, 71, 1131-1142.
    • (1992) Cell , vol.71 , pp. 1131-1142
    • Wichmann, H.1    Hengst, L.2    Gallwitz, D.3
  • 67
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.