메뉴 건너뛰기




Volumn 21, Issue 2, 1998, Pages 401-413

Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; SYNAPTOBREVIN; SYNTAXIN;

EID: 0032142949     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80549-8     Document Type: Article
Times cited : (179)

References (62)
  • 3
    • 0030807931 scopus 로고    scopus 로고
    • Coupled ER to golgi transport reconstituted with purified cytosolic proteins
    • Barlowe, C. (1997). Coupled ER to golgi transport reconstituted with purified cytosolic proteins. J. Cell Biol. 139, 1097-1108.
    • (1997) J. Cell Biol. , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 4
    • 0022071726 scopus 로고
    • A marker of early amacrine cell development in rat retina
    • Barnstable, C.J., Hofstein, R., and Akagawa, K. (1985). A marker of early amacrine cell development in rat retina. Brain Res. 352, 286-290.
    • (1985) Brain Res. , vol.352 , pp. 286-290
    • Barnstable, C.J.1    Hofstein, R.2    Akagawa, K.3
  • 6
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi, J., Chapman, E.R., Yamaski, S., Binz, T., Niemann, H., and Jahn, R. (1993b). Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12, 4821-4828.
    • (1993) EMBO J. , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamaski, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 7
    • 0028081451 scopus 로고
    • Absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission
    • Broadie, K., Bellen, H.J., Di Antonio, A., Littleton, J.T., and Schwarz, T.L. (1994). Absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission. Proc. Natl. Acad. Sci USA 91, 10727-10731.
    • (1994) Proc. Natl. Acad. Sci USA , vol.91 , pp. 10727-10731
    • Broadie, K.1    Bellen, H.J.2    Di Antonio, A.3    Littleton, J.T.4    Schwarz, T.L.5
  • 8
    • 0029093329 scopus 로고
    • Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila
    • Broadie, K., Prokop, A., Bellen, H.J., O'Kane, C.J., Schulze, K.L., and Sweeney, S.T. (1995). Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila. Neuron 15, 663-673.
    • (1995) Neuron , vol.15 , pp. 663-673
    • Broadie, K.1    Prokop, A.2    Bellen, H.J.3    O'Kane, C.J.4    Schulze, K.L.5    Sweeney, S.T.6
  • 9
    • 0028350057 scopus 로고
    • Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
    • Calakos, N., Bennett, M.K., Peterson, K.E., and Scheller, R.H. (1994). Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science 263, 1146-1149.
    • (1994) Science , vol.263 , pp. 1146-1149
    • Calakos, N.1    Bennett, M.K.2    Peterson, K.E.3    Scheller, R.H.4
  • 10
    • 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
  • 11
    • 0028970788 scopus 로고
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1. J. Biol. Chem. 270, 23667-23671.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    An, S.3    Jahn, R.4
  • 13
    • 0032521343 scopus 로고    scopus 로고
    • Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-synaptobrevin
    • Deitcher, D.L., Ueda, A., Stewart, B.A., Burgess, R.W., Kidokoro, Y., and Schwarz, T.L. (1998). Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-synaptobrevin. J. Neurosci. 18, 2028-2039.
    • (1998) J. Neurosci. , vol.18 , pp. 2028-2039
    • Deitcher, D.L.1    Ueda, A.2    Stewart, B.A.3    Burgess, R.W.4    Kidokoro, Y.5    Schwarz, T.L.6
  • 14
    • 0028351171 scopus 로고
    • The effect on synaptic physiology of synaptotagmin mutations in Drosophila
    • DiAntonio, A., and Schwarz, T.L. (1994). The effect on synaptic physiology of synaptotagmin mutations in Drosophila. Neuron 12, 909-920.
    • (1994) Neuron , vol.12 , pp. 909-920
    • DiAntonio, A.1    Schwarz, T.L.2
  • 15
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann, L., Hanson, P.I., Chapman, E.R., and Jahn, R. (1995). Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. EMBO J. 14, 224-231.
    • (1995) EMBO J. , vol.14 , pp. 224-231
    • Edelmann, L.1    Hanson, P.I.2    Chapman, E.R.3    Jahn, R.4
  • 16
    • 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
  • 18
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release - Four years of SNARE complexes
    • Hanson, P.I., Heuser, J.E., and Jahn, R. (1997a). Neurotransmitter release - four years of SNARE complexes. Curr. Opin. Neurobiol. 7, 310-315.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 19
    • 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., and Heuser, J.E. (1997b). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 20
    • 0027938531 scopus 로고
    • Mutations in the Drosophila rop gene suggest a function in general secretion and synaptic transmission
    • Harrison, S.D., Broadie, K., van de Goor, J., and Rubin, G.M. (1994). Mutations in the Drosophila rop gene suggest a function in general secretion and synaptic transmission. Neuron 13, 555-566.
    • (1994) Neuron , vol.13 , pp. 555-566
    • Harrison, S.D.1    Broadie, K.2    Van De Goor, J.3    Rubin, G.M.4
  • 21
    • 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
  • 22
    • 0014691624 scopus 로고
    • Abnormal electroretinograms in visual mutants of Drosophila
    • Hotta, Y., and Benzer, S. (1969). Abnormal electroretinograms in visual mutants of Drosophila. Nature 222, 351-354.
    • (1969) Nature , vol.222 , pp. 351-354
    • Hotta, Y.1    Benzer, S.2
  • 24
    • 0029058496 scopus 로고
    • Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation
    • Kee, Y., Lin, R.C., Hsu, S.-C., and Scheller, R.H. (1995). Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation. Neuron 14, 991-998.
    • (1995) Neuron , vol.14 , pp. 991-998
    • Kee, Y.1    Lin, R.C.2    Hsu, S.-C.3    Scheller, R.H.4
  • 25
    • 0029807825 scopus 로고    scopus 로고
    • Synaptic vesicles have two distinct recycling pathways
    • Koenig, J.H., and Ikeda, K. (1996). Synaptic vesicles have two distinct recycling pathways. J. Cell Biol. 135, 797-808.
    • (1996) J. Cell Biol. , vol.135 , pp. 797-808
    • Koenig, J.H.1    Ikeda, K.2
  • 26
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin, C.R., and Scheller, R.H. (1997). Structural organization of the synaptic exocytosis core complex. Neuron 19, 1087-1094.
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, C.R.1    Scheller, R.H.2
  • 28
    • 0027249801 scopus 로고
    • Expression of synaptotagmin in Drosophila reveals transport and localization of synaptic vesicles to the synapse
    • Littleton, J.T., Bellen, H.J., and Perin, M.S. (1993a). Expression of synaptotagmin in Drosophila reveals transport and localization of synaptic vesicles to the synapse. Development 118, 1077-1088.
    • (1993) Development , vol.118 , pp. 1077-1088
    • Littleton, J.T.1    Bellen, H.J.2    Perin, M.S.3
  • 30
    • 0027974130 scopus 로고
    • Calcium dependence of neurotransmitter release and rate of sponataneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • Littleton, J.T., Stern, M., Perin, M., and Bellen, H.J. (1994). Calcium dependence of neurotransmitter release and rate of sponataneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc. Natl. Acad. Sci. USA 91, 10888-10892.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10888-10892
    • Littleton, J.T.1    Stern, M.2    Perin, M.3    Bellen, H.J.4
  • 32
    • 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
  • 33
    • 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
  • 34
    • 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
  • 35
    • 0028802295 scopus 로고
    • Each domain of N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E.E., Bernstein, A., and Whiteheart, S.W. (1995). Each domain of N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 270, 29182-29188.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29182-29188
    • Nagiec, E.E.1    Bernstein, A.2    Whiteheart, S.W.3
  • 38
    • 0024966027 scopus 로고
    • Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stack
    • Orci, L., Malhotra, V., Amherdt, M., Serafini, T., and Rothman, J.E. (1989). Dissection of a single round of vesicular transport: sequential intermediates for intercisternal movement in the Golgi stack. Cell 56, 357-368.
    • (1989) Cell , vol.56 , pp. 357-368
    • Orci, L.1    Malhotra, V.2    Amherdt, M.3    Serafini, T.4    Rothman, J.E.5
  • 39
    • 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
  • 40
    • 0014691611 scopus 로고
    • Nonphototactic mutants in a study of vision in Drosophila
    • Pak, W.L., Grossfield, J., and White, N.V. (1969). Nonphototactic mutants in a study of vision in Drosophila. Nature 222, 351-354.
    • (1969) Nature , vol.222 , pp. 351-354
    • Pak, W.L.1    Grossfield, J.2    White, N.V.3
  • 43
    • 0019969545 scopus 로고
    • Synaptic vesicle activity instimulated and unstimulated photoreceptor axons of the housefly: A freeze fracture study
    • Saint Marie, R.L., and Carlson, S.D. (1982). Synaptic vesicle activity instimulated and unstimulated photoreceptor axons of the housefly: a freeze fracture study. J. Neurocytol. 11, 747-761.
    • (1982) J. Neurocytol. , vol.11 , pp. 747-761
    • Saint Marie, R.L.1    Carlson, S.D.2
  • 44
    • 0029058492 scopus 로고
    • Membrane trafficking in the presynaptic nerve terminal
    • Scheller, R.H. (1995). Membrane trafficking in the presynaptic nerve terminal. Neuron 14, 893-897.
    • (1995) Neuron , vol.14 , pp. 893-897
    • Scheller, R.H.1
  • 46
    • 0029589647 scopus 로고
    • A possible docking and fusion particle for synaptic transmission
    • Schiavo, G., Gmachl, M.J.S., Stenbeck, G., Söllner, T.H., and Rothman, J.E. (1995). A possible docking and fusion particle for synaptic transmission. Nature 378, 733-736.
    • (1995) Nature , vol.378 , pp. 733-736
    • Schiavo, G.1    Gmachl, M.J.S.2    Stenbeck, G.3    Söllner, T.H.4    Rothman, J.E.5
  • 47
    • 0028817584 scopus 로고
    • Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission
    • Schulze, K., Broadie, K., Perin, M., and Bellen, H.J. (1995). Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission. Cell 80, 311-320.
    • (1995) Cell , vol.80 , pp. 311-320
    • Schulze, K.1    Broadie, K.2    Perin, M.3    Bellen, H.J.4
  • 49
    • 0028595727 scopus 로고
    • Identification of a syntaxin-binding site on N-type calcium channels
    • Sheng, Z.-H., Rettig, J., Takahashi, M., and Catterall, W.A. (1994). Identification of a syntaxin-binding site on N-type calcium channels. Neuron 13, 1303-1313.
    • (1994) Neuron , vol.13 , pp. 1303-1313
    • Sheng, Z.-H.1    Rettig, J.2    Takahashi, M.3    Catterall, W.A.4
  • 50
    • 0004688543 scopus 로고
    • Neurophysiological defects in temperature-sensitive paralytic mutants of Drosophila melanogaster
    • Siddiqi, O., and Benzer, S. (1976). Neurophysiological defects in temperature-sensitive paralytic mutants of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 73, 3253-3257.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3253-3257
    • Siddiqi, O.1    Benzer, S.2
  • 51
    • 0028287470 scopus 로고
    • Neurotransmission: Harnessing fusion machinery at the synapse
    • Söllner, T., and Rothman, J.E. (1994). Neurotransmission: harnessing fusion machinery at the synapse. Trends Neurosci. 17, 344-348.
    • (1994) Trends Neurosci. , vol.17 , pp. 344-348
    • Söllner, T.1    Rothman, J.E.2
  • 52
    • 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., and Rothman, J.E. (1993a). 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.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 54
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. (1995). The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 55
    • 0028815501 scopus 로고
    • Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects
    • Sweeney, S.T., Broadie, K., Keane, J., Niemann, H., and O'Kane, C.J. (1995). Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects. Neuron 14, 341-351.
    • (1995) Neuron , vol.14 , pp. 341-351
    • Sweeney, S.T.1    Broadie, K.2    Keane, J.3    Niemann, H.4    O'Kane, C.J.5
  • 56
    • 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., and Wickner, W. (1998). 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) J. Cell Biol. , vol.140 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.3    Wickner, W.4
  • 57
    • 0029078068 scopus 로고
    • Redistribution of synaptic vesicles and their proteins in temperature-sensitive shibire(ts1) mutant Drosophila
    • van de Goor, J., Ramaswami, M., and Kelly, R. (1995). Redistribution of synaptic vesicles and their proteins in temperature-sensitive shibire(ts1) mutant Drosophila. Proc. Natl. Acad. Sci. USA 92, 5739-5743.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5739-5743
    • Van De Goor, J.1    Ramaswami, M.2    Kelly, R.3
  • 58
    • 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., von Mollard, G.F., 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, 637-645.
    • (1995) J. Cell Biol. , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.3    Chapman, E.R.4    Von Mollard, G.F.5    Jahn, R.6
  • 60
    • 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. USA 94, 3046-3051.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3046-3051
    • Weimbs, T.1    Low, S.H.2    Chapin, S.J.3    Mostov, K.E.4    Bucher, P.5    Hofmann, K.6
  • 61
    • 0028281387 scopus 로고
    • Paralysis and early death in cysteine string protein mutants of Drosophila
    • Zinsmaier, K.E., Eberle, K.K., Buchner, E., Walter, N., and Benzer, S. (1994). Paralysis and early death in cysteine string protein mutants of Drosophila. Science 263, 977-980.
    • (1994) Science , vol.263 , pp. 977-980
    • Zinsmaier, K.E.1    Eberle, K.K.2    Buchner, E.3    Walter, N.4    Benzer, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.