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Volumn 407, Issue 6801, 2000, Pages 153-159

Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

Author keywords

[No Author keywords available]

Indexed keywords

SNARE PROTEIN;

EID: 0034648836     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35025000     Document Type: Article
Times cited : (554)

References (50)
  • 1
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Söllner, T. et al. SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324 (1993).
    • (1993) Nature , vol.362 , pp. 318-324
    • Söllner, T.1
  • 2
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber, T. et al. SNAREpins: minimal machinery for membrane fusion. Cell 92, 759-772 (1998).
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 3
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. Mechanisms of intracellular protein transport. Nature 372, 55-63 (1994).
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 4
    • 0033602030 scopus 로고    scopus 로고
    • SNAREs and the secretory pathway-lessons from yeast
    • Pelham, H. R. SNAREs and the secretory pathway-lessons from yeast. Exp. Cell Res. 247, 1-8 (1999).
    • (1999) Exp. Cell Res. , vol.247 , pp. 1-8
    • Pelham, H.R.1
  • 5
    • 0033607279 scopus 로고    scopus 로고
    • Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain
    • Parlati, F. et al. Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain. Proc. Natl Acad. Sci. USA 96, 12565-12570 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12565-12570
    • Parlati, F.1
  • 6
    • 0033607182 scopus 로고    scopus 로고
    • Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs
    • Nickel, W. et al. Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc. Natl Acad. Sci. USA 96, 12571-12576 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12571-12576
    • Nickel, W.1
  • 8
    • 0034648797 scopus 로고    scopus 로고
    • Topological restriction of SNARE-dependent membrane fusion
    • Parlati, F. et al. Topological restriction of SNARE-dependent membrane fusion. Nature 407, 194-198 (2000).
    • (2000) Nature , vol.407 , pp. 194-198
    • Parlati, F.1
  • 9
    • 0034648771 scopus 로고    scopus 로고
    • Functional architecture of an intracellular t-SNARE
    • Fukuda, R. et al. Functional architecture of an intracellular t-SNARE. Nature 407, 198-202 (2000).
    • (2000) Nature , vol.407 , pp. 198-202
    • Fukuda, R.1
  • 10
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. 4 a resolution
    • Sutton, R. B., Fasshauer, D., Jahn, R. & Brunger, A. T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. 4 A resolution. Nature 395, 347-353 (1998).
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 11
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P. I., Roth, R., Morisaki, H., Jahn, R. & Heuser, J. E. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535 (1997).
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 12
    • 0030735370 scopus 로고    scopus 로고
    • Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation
    • Fasshauer, D., Otto, H., Eliason, W. K., Jahn, R. & Brunger, A. T. Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem. 272, 28036-28041 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3    Jahn, R.4    Brunger, A.T.5
  • 13
    • 0034631955 scopus 로고    scopus 로고
    • Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors
    • McNew, J. A. et al. Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J. Cell Biol. 150, 105-118 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 105-118
    • McNew, J.A.1
  • 14
    • 0031709722 scopus 로고    scopus 로고
    • Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p
    • Nicholson, K. L. et al. Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nature Struct. Biol. 5, 793-802 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 793-802
    • Nicholson, K.L.1
  • 15
    • 0033491695 scopus 로고    scopus 로고
    • Activity-dependent changes in partial VAMP complexes during neurotransmitter release
    • Hua, S. Y. & Charlton, M. P. Activity-dependent changes in partial VAMP complexes during neurotransmitter release. Nature Neurosci. 2, 1078-1083 (1999).
    • (1999) Nature Neurosci. , vol.2 , pp. 1078-1083
    • Hua, S.Y.1    Charlton, M.P.2
  • 16
    • 0033598965 scopus 로고    scopus 로고
    • Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis
    • Xu, T. et al. Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis. Cell 99, 713-722 (1999).
    • (1999) Cell , vol.99 , pp. 713-722
    • Xu, T.1
  • 17
    • 0033197735 scopus 로고    scopus 로고
    • The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion
    • McNew, J. A., Weber, T., Engelman, D. M., Söllner, T. H. & Rothman, J. E. The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion. Mol. Cell 4, 415-421 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 415-421
    • McNew, J.A.1    Weber, T.2    Engelman, D.M.3    Söllner, T.H.4    Rothman, J.E.5
  • 18
    • 0032404442 scopus 로고    scopus 로고
    • Model for structural similarity between different SNARE complexes based on sequence relationships
    • Weimbs, T., Mostov, K., Low, S. H. & Hofmann, K. A model for structural similarity between different SNARE complexes based on sequence relationships. Trends Cell. Biol. 8, 260-262 (1998).
    • (1998) Trends Cell. Biol. , vol.8 , pp. 260-262
    • Weimbs, T.1    Mostov, K.2    Low, S.H.3    Hofmann, K.A.4
  • 19
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald, P. et al. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 79, 245-258 (1994).
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1
  • 20
    • 0027527762 scopus 로고
    • Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport
    • Aalto, M. K., Ronne, H. & Keranen, S. Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. EMBO J. 12, 4095-4104 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4095-4104
    • Aalto, M.K.1    Ronne, H.2    Keranen, S.3
  • 21
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov, V., Govindan, B., Novick, P. & Gerst, J. E. Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74, 855-861 (1993).
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 22
    • 0026556288 scopus 로고
    • SNCI, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: Genetic interactions with the RAS and CAP genes
    • Gerst, J. E., Rodgers, L., Riggs, M. & Wigler, M. SNCI, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: genetic interactions with the RAS and CAP genes. Proc. Natl Acad. Sci. USA 89, 4338-4342 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4338-4342
    • Gerst, J.E.1    Rodgers, L.2    Riggs, M.3    Wigler, M.4
  • 23
    • 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., Hanson, P. I., Heuser, J. E. & Brennwald, P. 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 J. 17, 6200-6209 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6200-6209
    • Katz, L.1    Hanson, P.I.2    Heuser, J.E.3    Brennwald, P.4
  • 24
    • 0030959248 scopus 로고    scopus 로고
    • Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function
    • Gerst, J. E. Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function. J. Biol. Chem. 272, 16591-16598 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 16591-16598
    • Gerst, J.E.1
  • 25
    • 0031940772 scopus 로고    scopus 로고
    • Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast
    • Neiman, A. M. Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast. J. Cell Biol. 140, 29-37 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 29-37
    • Neiman, A.M.1
  • 26
    • 0030814115 scopus 로고    scopus 로고
    • Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport
    • McNew, J. A. et al. Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport. J. Biol. Chem. 272, 17776-17783 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 17776-17783
    • McNew, J.A.1
  • 27
    • 0025282485 scopus 로고
    • BET1, BOS1, and SEC22 art members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex
    • Newman, A. P., Shim, J. & Ferro-Novick, S. BET1, BOS1, and SEC22 art members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol. Cell. Biol. 10, 3405-3414 (1990).
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3405-3414
    • Newman, A.P.1    Shim, J.2    Ferro-Novick, S.3
  • 28
    • 0032516856 scopus 로고    scopus 로고
    • SNAREs and membrane fusion in the Golgi apparatus
    • Nichols, B. J. & Pelham, H. R. SNAREs and membrane fusion in the Golgi apparatus. Biochim. Biophys. Acta 1404, 9-31 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 9-31
    • Nichols, B.J.1    Pelham, H.R.2
  • 29
    • 0029024860 scopus 로고
    • A SNARE-like protein required for traffic through the Golgi complex
    • Banfield, D. K., Lewis, M. J. & Pelham, H. R. A SNARE-like protein required for traffic through the Golgi complex. Nature 375, 806-809 (1995).
    • (1995) Nature , vol.375 , pp. 806-809
    • Banfield, D.K.1    Lewis, M.J.2    Pelham, H.R.3
  • 30
    • 0032508558 scopus 로고    scopus 로고
    • Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport
    • McNew, J. A. et al. Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport. FEBS Lett. 435, 89-95 (1998).
    • (1998) FEBS Lett. , vol.435 , pp. 89-95
    • McNew, J.A.1
  • 31
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Søgaard, M. et al. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 78, 937-948 (1994).
    • (1994) Cell , vol.78 , pp. 937-948
    • Søgaard, M.1
  • 32
    • 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. Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic. Mol. Biol. Cell 8, 2659-2676 (1997).
    • (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
  • 33
    • 0030990122 scopus 로고    scopus 로고
    • The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p
    • von Mollard, G. F., Nothwehr, S. F. & Stevens, T. H. 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).
    • (1997) J. Cell Biol. , vol.137 , pp. 1511-1524
    • Von Mollard, G.F.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 34
    • 0032496164 scopus 로고    scopus 로고
    • Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures
    • Abeliovich, H., Grote, E., Novick, P. & Ferro-Novick, S. Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. J. Biol. Chem. 273, 11719-11727 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 11719-11727
    • Abeliovich, H.1    Grote, E.2    Novick, P.3    Ferro-Novick, S.4
  • 35
    • 0001206086 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae v-SNARE Vtilp is required for multiple membrane transport pathways to the vacuole
    • Fischer von Mollard, G. & Stevens, T. H. The Saccharomyces cerevisiae v-SNARE Vtilp is required for multiple membrane transport pathways to the vacuole. Mol. Biol. Cell 10, 1719-1732 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1719-1732
    • Fischer Von Mollard, G.1    Stevens, T.H.2
  • 36
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T. & Jahn, R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl Acad. Sci. USA 95, 15781-15786 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 37
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W. & Haas, A. Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94 (1996).
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 38
    • 0031942615 scopus 로고    scopus 로고
    • A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
    • Ungermann, C., Nichols, B. J., Pelham, H. R. & Wickner, W. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J. Cell Biol. 140, 61-69 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.3    Wickner, W.4
  • 39
    • 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. W., Scheller, R. H. & Rothman, J. E. 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).
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 41
    • 0034729298 scopus 로고    scopus 로고
    • SNAREpins are functionally resistant to disruption by NSF and αSNAP
    • Weber, T. et al. SNAREpins are functionally resistant to disruption by NSF and αSNAP. J. Cell Biol. 149, 1063-1072 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 1063-1072
    • Weber, T.1
  • 42
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J. C. & Pelham, H. R. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16, 1832-1841 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.2
  • 43
    • 0033179888 scopus 로고    scopus 로고
    • Membrane tethering in intracellular transport
    • Waters, M. G. & Pfeffer, S. R. Membrane tethering in intracellular transport. Curr. Opin. Cell Biol. 11, 453-459 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 453-459
    • Waters, M.G.1    Pfeffer, S.R.2
  • 44
    • 0033582905 scopus 로고    scopus 로고
    • Regulation of membrane trafficking: Structural insights from a Rab/ effector complex
    • Gonzalez, L. Jr. & Scheller, R. H. Regulation of membrane trafficking: structural insights from a Rab/ effector complex. Cell 96, 755-758 (1999).
    • (1999) Cell , vol.96 , pp. 755-758
    • Gonzalez L., Jr.1    Scheller, R.H.2
  • 45
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman, I. & Warren, G. The road taken: past and future foundations of membrane traffic. Cell 100, 99-112 (2000).
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 46
    • 0033523774 scopus 로고    scopus 로고
    • Regulated secretion from hemopoietic cells
    • Stinchcombe, J. C. & Griffiths, G. M. Regulated secretion from hemopoietic cells. J. Cell Biol. 147, 1-6 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1-6
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 47
    • 0033034407 scopus 로고    scopus 로고
    • Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties
    • Fasshauer, D., Antonin, W., Margittai, M., Pabst, S. & Jahn, R. Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties. J. Biol. Chem. 274, 15440-15446 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 15440-15446
    • Fasshauer, D.1    Antonin, W.2    Margittai, M.3    Pabst, S.4    Jahn, R.5
  • 48
    • 0033605147 scopus 로고    scopus 로고
    • SNARE interactions are not selective. Implications for membrane fusion specificity
    • Yang, B. et al. SNARE interactions are not selective. Implications for membrane fusion specificity. J. Biol. Chem. 274, 5649-5653 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 5649-5653
    • Yang, B.1
  • 49
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P. & Zerial, M. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9, 496-504 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 50
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W. & Weissmann, C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56, 502-514 (1973).
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2


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