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Volumn 2, Issue 2, 2001, Pages 98-106

Snare-mediated membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

EID: 0035256978     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35052017     Document Type: Review
Times cited : (920)

References (101)
  • 1
  • 2
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer, S. R. Transport-vesicle targeting: tethers before SNAREs. Nature Cell Biol. 1, 17-22 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 17-22
    • Pfeffer, S.R.1
  • 3
    • 0034130649 scopus 로고    scopus 로고
    • Priming in exocytosis: Attaining fusion-competence after vesicle docking
    • Klenchin, V. A. & Martin, T. F. Priming in exocytosis: attaining fusion-competence after vesicle docking. Biochimie 82, 399-407 (2000).
    • (2000) Biochimie , vol.82 , pp. 399-407
    • Klenchin, V.A.1    Martin, T.F.2
  • 4
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • Heidelberger, R., Heinemann, C., Neher, E. & Matthews, G. Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature 371, 513-515 (1994).
    • (1994) Nature , vol.371 , pp. 513-515
    • Heidelberger, R.1    Heinemann, C.2    Neher, E.3    Matthews, G.4
  • 5
    • 0032506349 scopus 로고    scopus 로고
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396, 575-580 (1998).
    • (1998) Nature , vol.396 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 6
    • 0024596794 scopus 로고
    • Calcium and GTP: Essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus
    • Beckers, C. J. & Balch, W. E. Calcium and GTP: essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus. J. Cell Biol. 108, 1245-1256 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 1245-1256
    • Beckers, C.J.1    Balch, W.E.2
  • 7
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo, M. I., Beron, W. & Stahl, P. D. Calmodulin regulates endosome fusion. J. Biol. Chem. 272, 7707-7712 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7707-7712
    • Colombo, M.I.1    Beron, W.2    Stahl, P.D.3
  • 8
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M. K., Calakos, N. & Scheller, R. H. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257, 255-259 (1992).
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 9
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler, G. A. et al. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109, 3039-3052 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1
  • 10
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble, W. S., Cowan, D. M. & Scheller, R. H. VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc. Natl Acad. Sci. USA 85, 4538-4542 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 11
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 Daltons present in small synaptic vesicles of rat brain
    • Baumert, M., Maycox, P. R., Navone, F., De Camilli, P. & Jahn, R. Synaptobrevin: an integral membrane protein of 18,000 Daltons present in small synaptic vesicles of rat brain. EMBO J. 8, 379-384 (1989).
    • (1989) EMBO J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 12
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C. & Schekman, R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21, 205-215 (1980).
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 13
    • 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
  • 14
    • 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., Brünger, 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    Brünger, A.T.3    Jahn, R.4
  • 15
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. & Südhof, T. C. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 16
    • 0033716880 scopus 로고    scopus 로고
    • SNAREs contribute to the specificity of membrane fusion
    • Scales, S. J. et al. SNAREs contribute to the specificity of membrane fusion. Neuron 26, 457-464 (2000). This is the first study in which many cognate and non-cognate SNARE coils were tested for their ability to function in a specific cellular fusion step.
    • (2000) Neuron , vol.26 , pp. 457-464
    • Scales, S.J.1
  • 18
    • 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
  • 19
    • 0034648836 scopus 로고    scopus 로고
    • Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
    • McNew, J. A. et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature 407, 153-159 (2000). This is a thorough study of SNARE fusion specificity in the synthetic liposome fusion model.
    • (2000) Nature , vol.407 , pp. 153-159
    • McNew, J.A.1
  • 20
    • 0032555126 scopus 로고    scopus 로고
    • Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly
    • Fasshauer, D., Eliason, W. K., Brünger, A. T. & Jahn, R. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry 37, 10354-10362 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1    Eliason, W.K.2    Brünger, A.T.3    Jahn, R.4
  • 21
    • 0032079715 scopus 로고    scopus 로고
    • Protease resistance of syntaxin-SNAP-25-VAMP complexes. Implications for assembly and structure
    • Poirier, M. A. et al. Protease resistance of syntaxin-SNAP-25-VAMP complexes. Implications for assembly and structure. J. Biol. Chem. 273, 11370-11377 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 11370-11377
    • Poirier, M.A.1
  • 22
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T. et al. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1
  • 23
    • 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
  • 24
    • 0027932454 scopus 로고
    • Specificity and regulation of a synaptic vesicle docking complex
    • Pevsner, J. et al. Specificity and regulation of a synaptic vesicle docking complex. Neuron 13, 353-361 (1994).
    • (1994) Neuron , vol.13 , pp. 353-361
    • Pevsner, J.1
  • 25
    • 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
  • 26
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin, R. C. & Scheller, R. H. Structural organization of the synaptic exocytosis core complex. Neuron 19, 1087-1094 (1997).
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 27
    • 0031668972 scopus 로고    scopus 로고
    • The synaptic SNARE complex is a parallel four-stranded helical bundle
    • Poirier, M. A. et al. The synaptic SNARE complex is a parallel four-stranded helical bundle. Nature Struct. Biol. 5, 765-769 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 765-769
    • Poirier, M.A.1
  • 28
    • 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. & Rothman, J. E. 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).
    • (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
  • 29
    • 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. & Rothman, J. E. SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell 61, 709-721 (1990).
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 30
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C. U., Steinmann, D., Whiteheart, S. W. & Weis, W. I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536 (1998).
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 31
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R. C., Hanson, P. I., Jahn, R. & Brünger, A. T. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nature Struct. Biol. 5, 803-611 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 803-1611
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brünger, A.T.4
  • 32
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20S particles consisting of NSF, SNAPs, and SNARE complexes
    • Hohl, T. M. et al. Arrangement of subunits in 20S particles consisting of NSF, SNAPs, and SNARE complexes. Mol. Cell 2, 539-548 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 539-548
    • Hohl, T.M.1
  • 33
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein
    • May, A. P., Misura, K. M., Whiteheart, S. W. & Weis, W. I. Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nature Cell Biol. 1, 175-182 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 175-182
    • May, A.P.1    Misura, K.M.2    Whiteheart, S.W.3    Weis, W.I.4
  • 34
    • 0033165864 scopus 로고    scopus 로고
    • NSF N-terminal domain crystal structure: Models of NSF function
    • Yu, R. C., Jahn, R. & Brünger, A. T. NSF N-terminal domain crystal structure: models of NSF function. Mol. Cell 4, 97-107 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 97-107
    • Yu, R.C.1    Jahn, R.2    Brünger, A.T.3
  • 35
    • 0033165863 scopus 로고    scopus 로고
    • Crystal structure of the vesicular transport protein Sec17: Implications for SNAP function in SNARE complex disassembly
    • Rice, L. M. & Brünger, A. T. Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly. Mol. Cell 4, 85-95 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 85-95
    • Rice, L.M.1    Brünger, A.T.2
  • 36
    • 0032544441 scopus 로고    scopus 로고
    • Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A
    • Fernandez, I. et al. Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A. Cell 94, 841-849 (1998).
    • (1998) Cell , vol.94 , pp. 841-849
    • Fernandez, I.1
  • 37
    • 0034713847 scopus 로고    scopus 로고
    • Structural analysis of the neuronal SNARE protein syntaxin-1A
    • Lerman, J. C., Robblee, J., Fairman, R. & Hughson, F. M. Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochemistry 39, 8470-8479 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8470-8479
    • Lerman, J.C.1    Robblee, J.2    Fairman, R.3    Hughson, F.M.4
  • 38
    • 0028350057 scopus 로고
    • Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
    • Calakos, N., Bennett, M. K., Peterson, K. E. & Scheller, R. H. Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science 263, 1146-1149 (1994).
    • (1994) Science , vol.263 , pp. 1146-1149
    • Calakos, N.1    Bennett, M.K.2    Peterson, K.E.3    Scheller, R.H.4
  • 39
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1 a complex
    • Misura, K. M. S., Scheller, R. H. & Weis, W. I. Three-dimensional structure of the neuronal-Sec1-syntaxin 1 a complex. Nature 404, 355-362 (2000). The structure revealed that a pronounced conformational change of syntaxin occurs before fusion.
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.S.1    Scheller, R.H.2    Weis, W.I.3
  • 40
    • 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
  • 41
    • 0033607279 scopus 로고    scopus 로고
    • Rapid and efficient fusion of phospholipid vesicles by the α-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 α-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
  • 42
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C. A. & Südhof, T. C. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366, 347-351 (1993).
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 44
    • 0033575749 scopus 로고    scopus 로고
    • A conformational switch in syntaxin during exocytosis: Role of munc18
    • Dulubova, I. et al. A conformational switch in syntaxin during exocytosis: role of munc18. EMBO J. 18, 4372-4382 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4372-4382
    • Dulubova, I.1
  • 45
    • 0033574464 scopus 로고    scopus 로고
    • 2+ and drives membrane fusion
    • 2+ and drives membrane fusion. Cell 97, 165-174 (1999). This was the first systematic structure-function analysis of a SNARE protein. It provided the first piece of direct functional evidence in a physiological system that SNAREs drive membrane fusion.
    • (1999) Cell , vol.97 , pp. 165-174
    • Chen, Y.A.1    Scales, S.J.2    Patel, S.M.3    Doung, Y.C.4    Scheller, R.H.5
  • 46
    • 0034648771 scopus 로고    scopus 로고
    • Functional architecture of an intracellular membrane t-SNARE
    • Fukuda, R. et al. Functional architecture of an intracellular membrane t-SNARE. Nature 407, 198-202 (2000).
    • (2000) Nature , vol.407 , pp. 198-202
    • Fukuda, R.1
  • 47
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink, L. A., Trimble, W. S. & Scheller, R. H. Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 264, 11061-11064 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061-11064
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, R.H.3
  • 48
    • 0029041786 scopus 로고
    • Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuro-exocytosis
    • Cornille, F., Deloye, F., Fournie-Zaluski, M. C., Roques, B. P. & Poulain, B. Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuro-exocytosis. J. Biol. Chem. 270, 16826-16832 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 16826-16832
    • Cornille, F.1    Deloye, F.2    Fournie-Zaluski, M.C.3    Roques, B.P.4    Poulain, B.5
  • 49
    • 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). The authors proposed a detailed kinetic model of SNARE-mediated fusion reaction based on quantitative electrophysiological analyses.
    • (1999) Cell , vol.99 , pp. 713-722
    • Xu, T.1
  • 50
    • 0033057030 scopus 로고    scopus 로고
    • A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains
    • Margittai, M., Otto, H. & Jahn, R. A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains. FEBS Lett. 446, 40-44 (1999).
    • (1999) FEBS Lett. , vol.446 , pp. 40-44
    • Margittai, M.1    Otto, H.2    Jahn, R.3
  • 51
    • 0034625384 scopus 로고    scopus 로고
    • A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins
    • Laage, R., Rohde, J., Brosig, B. & Langosch, D. A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins. J. Biol. Chem. 275, 17481-17487 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 17481-17487
    • Laage, R.1    Rohde, J.2    Brosig, B.3    Langosch, D.4
  • 52
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R. B., Fasshauer, D., Jahn, R. & Brünger, A. T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353 (1998). Provided the first high-resolution crystal structure of a SNARE complex, which was instrumental in elucidating the function of SNARE proteins.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brünger, A.T.4
  • 53
    • 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
  • 54
    • 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, 105-117 (2000). Taking advantage of the liposome fusion system (first described in reference 58), the authors delved deep into the mechanisms by which the SNAREs fuse two lipid bilayers.
    • (2000) J. Cell Biol. , vol.150 , pp. 105-117
    • McNew, J.A.1
  • 55
    • 0032142949 scopus 로고    scopus 로고
    • Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly
    • Littleton, J. T. et al. Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Neuron 21, 401-413 (1998).
    • (1998) Neuron , vol.21 , pp. 401-413
    • Littleton, J.T.1
  • 56
    • 0026664632 scopus 로고
    • Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins
    • Hay, J. C. & Martin, T. F. Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins. J. Cell Biol. 119, 139-151 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 139-151
    • Hay, J.C.1    Martin, T.F.2
  • 57
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu, T., Binz, T., Niemann, H. & Neher, E. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nature Neurosci. 1, 192-200 (1998).
    • (1998) Nature Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 58
    • 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
  • 59
    • 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
  • 60
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann, C., Sato, K. & Wickner, W. Defining the functions of trans-SNARE pairs. Nature 396, 543-548 (1998). The controversy concerning SNARE function was heavily fuelled by this report, which concluded that SNAREs are not directly involved in the membrane fusion process.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 61
    • 0032509210 scopus 로고    scopus 로고
    • Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion
    • Tahara, M. et al. Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion. J. Biol. Chem. 273, 33667-33673 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33667-33673
    • Tahara, M.1
  • 63
    • 0033551865 scopus 로고    scopus 로고
    • Control of the terminal step of intracellular membrane fusion by protein phosphatase 1
    • Peters, C. et al. Control of the terminal step of intracellular membrane fusion by protein phosphatase 1. Science 285, 1084-1087 (1999).
    • (1999) Science , vol.285 , pp. 1084-1087
    • Peters, C.1
  • 65
    • 0028978947 scopus 로고
    • Distinct effects of α-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis
    • Chamberlain, L. H., Roth, D., Morgan, A. & Burgoyne, R. D. Distinct effects of α-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis. J. Cell Biol. 130, 1063-1070 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 1063-1070
    • Chamberlain, L.H.1    Roth, D.2    Morgan, A.3    Burgoyne, R.D.4
  • 66
    • 0034662499 scopus 로고    scopus 로고
    • 2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin
    • 2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin-and phospholipid-binding domain of synaptobrevin. Proc. Natl Acad. Sci. USA 97, 9695-9700 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9695-9700
    • Quetglas, S.1    Leveque, C.2    Miquelis, R.3    Sato, K.4    Seagar, M.5
  • 67
    • 0033230605 scopus 로고    scopus 로고
    • Disruption of Rab3-calmodulin interaction, but not other effector interactions, prevents Rab3 inhibition of exocytosis
    • Coppola, T. et al. Disruption of Rab3-calmodulin interaction, but not other effector interactions, prevents Rab3 inhibition of exocytosis. EMBO J. 18, 5885-5891 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5885-5891
    • Coppola, T.1
  • 68
    • 0030448343 scopus 로고    scopus 로고
    • Ultrafast exocytosis elicited by calcium current in synaptic terminals of retinal bipolar neurons
    • Mennerick, S. & Matthews, G. Ultrafast exocytosis elicited by calcium current in synaptic terminals of retinal bipolar neurons. Neuron 17, 1241-1249 (1996).
    • (1996) Neuron , vol.17 , pp. 1241-1249
    • Mennerick, S.1    Matthews, G.2
  • 69
    • 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). This paper presents compelling evidence that partially assembled SNARE complexes exist.
    • (1999) Nature Neurosci. , vol.2 , pp. 1078-1083
    • Hua, S.Y.1    Charlton, M.P.2
  • 70
    • 0029811998 scopus 로고    scopus 로고
    • Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins
    • Pellizzari, R. et al. Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins. J. Biol. Chem. 271, 20353-20358 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 20353-20358
    • Pellizzari, R.1
  • 71
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments
    • Foran, P., Shone, C. C. & Dolly, J. O. Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments. Biochemistry 33, 15365-15374 (1994).
    • (1994) Biochemistry , vol.33 , pp. 15365-15374
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 72
    • 0031898897 scopus 로고    scopus 로고
    • RAB3 and synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert, M. & Südhof, T. C. RAB3 and synaptotagmin: the yin and yang of synaptic membrane fusion. Annu. Rev. Neurosci. 21, 75-95 (1998).
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 75-95
    • Geppert, M.1    Südhof, T.C.2
  • 73
    • 0033213302 scopus 로고    scopus 로고
    • 2+ and assembly with the core SNARE complex onto membranes
    • 2+ and assembly with the core SNARE complex onto membranes. Neuron 24, 363-376 (1999)
    • (1999) Neuron , vol.24 , pp. 363-376
    • Davis, A.F.1
  • 76
    • 0034605096 scopus 로고    scopus 로고
    • 2+-sensing module essential for exocytosis
    • 2+-sensing module essential for exocytosis. J. Cell Biol. 150, 1125-1136 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 1125-1136
    • Desai, R.C.1
  • 78
    • 0030222281 scopus 로고    scopus 로고
    • The fusion pore and mechanisms of biological membrane fusion
    • Monck, J. R. & Fernandez, J. M. The fusion pore and mechanisms of biological membrane fusion. Curr. Opin. Cell Biol. 8, 524-533 (1996).
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 524-533
    • Monck, J.R.1    Fernandez, J.M.2
  • 79
    • 0030943586 scopus 로고    scopus 로고
    • Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion
    • Lee, J. & Lentz, B. R. Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion. Biochemistry 36, 6251-6259 (1997).
    • (1997) Biochemistry , vol.36 , pp. 6251-6259
    • Lee, J.1    Lentz, B.R.2
  • 80
    • 0019305230 scopus 로고
    • Arrest of membrane fusion events in mast cells by quick-freezing
    • Chandler, D. E. & Heuser, J. E. Arrest of membrane fusion events in mast cells by quick-freezing. J. Cell Biol. 86, 666-674 (1980).
    • (1980) J. Cell Biol. , vol.86 , pp. 666-674
    • Chandler, D.E.1    Heuser, J.E.2
  • 81
    • 0023238873 scopus 로고
    • Currents through the fusion pore that forms during exocytosis of a secretory vesicle
    • Breckenridge, L. J. & Almers, W. Currents through the fusion pore that forms during exocytosis of a secretory vesicle. Nature 328, 814-817 (1987).
    • (1987) Nature , vol.328 , pp. 814-817
    • Breckenridge, L.J.1    Almers, W.2
  • 82
    • 0025284844 scopus 로고
    • Transmitter release from synapses: Does a preassembled fusion pore initiate exocytosis?
    • Almers, W. & Tse, F. W. Transmitter release from synapses: does a preassembled fusion pore initiate exocytosis? Neuron 4, 813-818 (1990).
    • (1990) Neuron , vol.4 , pp. 813-818
    • Almers, W.1    Tse, F.W.2
  • 83
    • 0028353472 scopus 로고
    • The exocytotic fusion pore and neurotransmitter release
    • Monck, J. R. & Fernandez, J. M. The exocytotic fusion pore and neurotransmitter release. Neuron 12, 707-716 (1994).
    • (1994) Neuron , vol.12 , pp. 707-716
    • Monck, J.R.1    Fernandez, J.M.2
  • 84
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel, J. J. & Wiley, D. C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95, 871-874 (1998).
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 85
    • 0031240001 scopus 로고    scopus 로고
    • Enveloped viruses: A common mode of membrane fusion?
    • Hughson, F. M. Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7, 565-569 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 565-569
    • Hughson, F.M.1
  • 86
    • 0021347134 scopus 로고
    • Effects of divalent cations, temperature, osmotic pressure gradient, and vesicle curvature on phosphatidylserine vesicle fusion
    • Ohki, S. Effects of divalent cations, temperature, osmotic pressure gradient, and vesicle curvature on phosphatidylserine vesicle fusion. J. Membr. Biol. 77, 265-275 (1984).
    • (1984) J. Membr. Biol. , vol.77 , pp. 265-275
    • Ohki, S.1
  • 87
    • 0034710645 scopus 로고    scopus 로고
    • Intracellular calcium dependence of transmitter release rates at a fast central synapse
    • Schneggenburger, R. & Neher, E. Intracellular calcium dependence of transmitter release rates at a fast central synapse. Nature 406, 889-892 (2000).
    • (2000) Nature , vol.406 , pp. 889-892
    • Schneggenburger, R.1    Neher, E.2
  • 88
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon, H. T., Missler, M., Li, C. & Südhof, T. C. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 83, 111-119 (1995).
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Südhof, T.C.4
  • 89
    • 17344376286 scopus 로고    scopus 로고
    • Tomosyn: A syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process
    • Fujita, Y. et al. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process. Neuron 20, 905-915 (1998).
    • (1998) Neuron , vol.20 , pp. 905-915
    • Fujita, Y.1
  • 90
    • 0031052719 scopus 로고    scopus 로고
    • Hrs-2 is an ATPase implicated in calcium-regulated secretion
    • Bean, A. J., Seifert, R., Chen, Y. A., Sacks, R. & Scheller, R. H. Hrs-2 is an ATPase implicated in calcium-regulated secretion. Nature 385, 826-829 (1997).
    • (1997) Nature , vol.385 , pp. 826-829
    • Bean, A.J.1    Seifert, R.2    Chen, Y.A.3    Sacks, R.4    Scheller, R.H.5
  • 91
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi, J. M., Mochida, S. & Sheng, Z. H. Snapin: a SNARE-associated protein implicated in synaptic transmission. Nature Neurosci. 2, 119-124 (1999).
    • (1999) Nature Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 92
    • 0034073884 scopus 로고    scopus 로고
    • Syntaphilin: A syntaxin-1 clamp that controls SNARE assembly
    • Lao, G. et al. Syntaphilin: a syntaxin-1 clamp that controls SNARE assembly. Neuron 25, 191-201 (2000).
    • (2000) Neuron , vol.25 , pp. 191-201
    • Lao, G.1
  • 93
    • 18544399674 scopus 로고    scopus 로고
    • Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release
    • Betz, A. et al. Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release. Neuron 21, 123-136 (1998).
    • (1998) Neuron , vol.21 , pp. 123-136
    • Betz, A.1
  • 94
    • 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. & Haas, A. Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94 (1996). This is the key paper that established the current view that α-SNAP and NSF function after fusion.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 95
    • 0028263696 scopus 로고
    • A post-docking role for synaptobrevin in synaptic vesicle fusion
    • Hunt, J. M. et al. A post-docking role for synaptobrevin in synaptic vesicle fusion. Neuron 12, 1269-1279 (1994).
    • (1994) Neuron , vol.12 , pp. 1269-1279
    • Hunt, J.M.1
  • 96
    • 0028817584 scopus 로고
    • Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission
    • Schulze, K. L., Broadie, K., Perin, M. S. & Bellen, H. J. Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission. Cell 80, 311-320 (1995).
    • (1995) Cell , vol.80 , pp. 311-320
    • Schulze, K.L.1    Broadie, K.2    Perin, M.S.3    Bellen, H.J.4
  • 97
    • 0029093329 scopus 로고
    • Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila
    • Broadie, K. et al. Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila. Neuron 15, 663-673 (1995).
    • (1995) Neuron , vol.15 , pp. 663-673
    • Broadie, K.1
  • 98
    • 0034669052 scopus 로고    scopus 로고
    • Exocytosis requires asymmetry in the central layer of the SNARE complex
    • Ossig, R. et al. Exocytosis requires asymmetry in the central layer of the SNARE complex. EMBO J. 19, 6000-6010 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6000-6010
    • Ossig, R.1
  • 99
    • 0033749565 scopus 로고    scopus 로고
    • Testing the 3Q:1R 'rule': Mutational analysis of the ionic 'zero' layer in the yeast exocytic SNARE complex reveals no requirement for arginine
    • Katz, L. & Brennwald, P. Testing the 3Q:1R 'rule': mutational analysis of the ionic 'zero' layer in the yeast exocytic SNARE complex reveals no requirement for arginine. Mol. Biol. Cell 11, 3849-3858 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3849-3858
    • Katz, L.1    Brennwald, P.2
  • 100
    • 0342751280 scopus 로고    scopus 로고
    • Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25
    • Wei, S. et al. Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25. EMBO J. 19, 1279-1289 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1279-1289
    • Wei, S.1
  • 101
    • 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


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