메뉴 건너뛰기




Volumn 2, Issue 5, 1998, Pages 539-548

Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MEMBRANE PROTEIN; MYC PROTEIN; N ETHYLMALEIMIDE SENSITIVE FACTOR; NERVE PROTEIN; NSF PROTEIN, RAT; PHOTOPROTEIN; SNARE PROTEIN; SOLUBLE N ETHYLMALEIMIDE SENSITIVE FACTOR ATTACHMENT PROTEIN; SYNAPTOBREVIN; SYNTAXIN; VESICULAR TRANSPORT PROTEIN;

EID: 0032214690     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80153-7     Document Type: Article
Times cited : (109)

References (61)
  • 1
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard, R.J., Morgan, A., and Burgoyne, R.D. (1997). Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis. J. Cell Biol. 139, 875-883.
    • (1997) J. Cell Biol. , vol.139 , pp. 875-883
    • Barnard, R.J.1    Morgan, A.2    Burgoyne, R.D.3
  • 2
    • 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., and Jahn, R. (1989). Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J. 8, 379-384.
    • (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
  • 3
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M.K., Calakos, N., and Scheller, R.H. (1992). Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257, 255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 5
    • 0025286486 scopus 로고
    • Purification of three related peripheral membrane proteins needed for vesicular transport
    • Clary, D.O., and Rothman, J.E. (1990). Purification of three related peripheral membrane proteins needed for vesicular transport. J. Biol. Chem. 265, 10109-10117.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10109-10117
    • Clary, D.O.1    Rothman, J.E.2
  • 6
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong, H., O'Brien, R.J., Tung, E.T., Lanahan, A.A., Worley, P.F, and Huganir, R.L. (1997). GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386, 279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Tung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 7
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink, L.A., Trimble, W.S., and Scheller, R.H. (1989). Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 264, 11061-11064.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061-11064
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, R.H.3
  • 8
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G.I., Lewis, G.K., Ramsay, G., and Bishop, J.M. (1985). Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5, 3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 9
    • 0017917406 scopus 로고
    • The use of singlet-singlet energy transfer to study macromolecular assemblies
    • Fairclough, R.H., and Cantor, C.R. (1978). The use of singlet-singlet energy transfer to study macromolecular assemblies. Methods Enzymol. 48, 347-379.
    • (1978) Methods Enzymol. , vol.48 , pp. 347-379
    • Fairclough, R.H.1    Cantor, C.R.2
  • 10
    • 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., and Jahn, R. (1998). Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry 37, 10354-10362.
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1    Eliason, W.K.2    Brünger, A.T.3    Jahn, R.4
  • 12
    • 0038843642 scopus 로고    scopus 로고
    • Multivariate statistical analysis and classification of images
    • San Diego, CA: Academic Press
    • Frank, J. (1996). Multivariate statistical analysis and classification of images. In Three Dimensional Electron Microscopy of Macromolecular Assemblies. (San Diego, CA: Academic Press), pp. 121-182.
    • (1996) Three Dimensional Electron Microscopy of Macromolecular Assemblies , pp. 121-182
    • Frank, J.1
  • 14
    • 0029075363 scopus 로고
    • The N-ethylmaleimide sensitive fusion protein and α-SNAP induce a conformational change in syntaxin
    • Hanson, P.I., Otto, H., Barton, N., and Jahn, R. (1995). The N-ethylmaleimide sensitive fusion protein and α-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270, 16955-16961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
  • 15
    • 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. (1997a). 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
  • 16
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release - Four years of SNARE complexes
    • Hanson, P.I., Heuser, J.E., and Jahn, R. (1997b). 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
  • 17
    • 0030890594 scopus 로고    scopus 로고
    • Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Hay, J.C., Chao, D.S., Kuo, C.S., and Scheller, R.H. (1997). Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Cell 89, 149-158.
    • (1997) Cell , vol.89 , pp. 149-158
    • Hay, J.C.1    Chao, D.S.2    Kuo, C.S.3    Scheller, R.H.4
  • 18
    • 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
  • 19
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi, T., Yamasaki, S., Nauenburg, S., Binz, T., and Niemann, H. (1995). Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14, 2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 20
    • 0029879294 scopus 로고    scopus 로고
    • The EM program package: A platform for image processing in biological electron microscopy
    • Hegerl, R. (1996). The EM program package: a platform for image processing in biological electron microscopy. J. Struct. Biol. 116, 30-34.
    • (1996) J. Struct. Biol. , vol.116 , pp. 30-34
    • Hegerl, R.1
  • 21
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R., and Tsien, R.Y. (1996). Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6, 178-182.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 22
    • 0026471991 scopus 로고
    • The 25 kDa 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., Wilson, M.C., and Skene, J.H.P. (1992). The 25 kDa 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    Wilson, M.C.3    Skene, J.H.P.4
  • 24
    • 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., and Weis, W.I. (1998). Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 25
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin, R.C., 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, R.C.1    Scheller, R.H.2
  • 26
    • 0028963427 scopus 로고
    • Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity α-SNAP binding site
    • McMahon, H.T., and Südhof, T.C. (1995). Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity α-SNAP binding site. J. Biol. Chem. 270, 2213-2217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2213-2217
    • McMahon, H.T.1    Südhof, T.C.2
  • 28
    • 0028802295 scopus 로고
    • Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E.E., Bernstein, A., and Whiteheart, S.W. (1995). Each domain of the 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
  • 32
    • 0024828306 scopus 로고
    • The Identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler, G.A., Higgins, G.A., Hart, R.A., Battenberg, E., Billingsley, M., Bloom, F.E., and Wilson, M.C. (1989). The Identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109, 3039-3052.
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 34
    • 0032489507 scopus 로고    scopus 로고
    • Organelle membrane fusion: A novel function for the syntaxin homolog Ufe1p in ER membrane fusion
    • Patel, S.K., Indig, F.E., Olivieri, N., Levine, N.D., and Latterich, M. (1998). Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion. Cell 92, 611-620.
    • (1998) Cell , vol.92 , pp. 611-620
    • Patel, S.K.1    Indig, F.E.2    Olivieri, N.3    Levine, N.D.4    Latterich, M.5
  • 35
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters, J.M., Walsh, M.J., and Franke, W.W. (1990). An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J. 9, 1757-1767.
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 38
    • 0032079715 scopus 로고    scopus 로고
    • Protease resistance of syntaxin/ SNAP-25/VAMP complexes. Implications for assembly and structure
    • Poirier, M.A., Hao, J.C., Malkus, P.N., Chan, C., Moore, M.F., King, D.S., and Bennett, M.K. (1998a). Protease resistance of syntaxin/ SNAP-25/VAMP complexes. Implications for assembly and structure. J. Biol. Chem. 273, 11370-11377.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11370-11377
    • Poirier, M.A.1    Hao, J.C.2    Malkus, P.N.3    Chan, C.4    Moore, M.F.5    King, D.S.6    Bennett, M.K.7
  • 40
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille, C., Kondo, H., Newman, R., Hui, N., Freemont, P., and Warren, G. (1998). Syntaxin 5 is a common component of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92, 603-610.
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, P.5    Warren, G.6
  • 41
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 42
    • 0032584707 scopus 로고    scopus 로고
    • Functional reconstitution of ypt7p GTPase and a purified vacuole SNARE complex
    • Sato, K., and Wickner, W. (1998). Functional reconstitution of ypt7p GTPase and a purified vacuole SNARE complex. Science 281, 700-702.
    • (1998) Science , vol.281 , pp. 700-702
    • Sato, K.1    Wickner, W.2
  • 43
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton, W.O., and Baumeister, W. (1982). The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsci. 127, 127-138.
    • (1982) J. Microsci. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 44
    • 0029945635 scopus 로고    scopus 로고
    • Semper: Distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system
    • Saxton, W.O. (1996). Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system. J. Struct. Biol. 116, 230-236.
    • (1996) J. Struct. Biol. , vol.116 , pp. 230-236
    • Saxton, W.O.1
  • 45
  • 47
    • 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. (1993b). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 48
    • 0032143945 scopus 로고    scopus 로고
    • Interaction of the N-ethylmalelmlde-sensitive factor with AMPA receptors
    • Song, I., Kamboj, S., Xia, J., Dong, H., Liao, D, and Huganir, R.L. (1998). Interaction of the N-ethylmalelmlde-sensitive factor with AMPA receptors. Neuron 21, 393-400.
    • (1998) Neuron , vol.21 , pp. 393-400
    • Song, I.1    Kamboj, S.2    Xia, J.3    Dong, H.4    Liao, D.5    Huganir, R.L.6
  • 49
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978). Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 50
    • 15844394630 scopus 로고    scopus 로고
    • GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport
    • Subramaniam, V.N., Peter., F., Philp, R., Wong, S.W., and Hong, W. (1996). GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport. Science 252, 1161-1163.
    • (1996) Science , vol.252 , pp. 1161-1163
    • Subramaniam, V.N.1    Peter, F.2    Philp, R.3    Wong, S.W.4    Hong, W.5
  • 51
    • 0030881792 scopus 로고    scopus 로고
    • N-ethylmaleimide-sensitive factor (NSF) and α-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-Syntaxin 5 Golgi SNAP receptor (SNARE) complexes
    • Subramaniam, V.N., Loh, E., and Hong, W. (1997). N-ethylmaleimide-sensitive factor (NSF) and α-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-Syntaxin 5 Golgi SNAP receptor (SNARE) complexes. J. Biol. Chem. 272, 25441-25444.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25441-25444
    • Subramaniam, V.N.1    Loh, E.2    Hong, W.3
  • 52
    • 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
  • 53
    • 0027474007 scopus 로고
    • Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport
    • Tagaya, M., Wilson, D.W., Brunner, M., Arango, N., and Rothman, J.E. (1993). Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268, 2662-2666.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2662-2666
    • Tagaya, M.1    Wilson, D.W.2    Brunner, M.3    Arango, N.4    Rothman, J.E.5
  • 54
    • 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
  • 55
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analysing the images of biological macro-molecules
    • van Heel, M., and Frank, J. (1981). Use of multivariate statistics in analysing the images of biological macro-molecules. Ultramicroscopy 6, 187-194.
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • Van Heel, M.1    Frank, J.2
  • 58
    • 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
  • 61
    • 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., and Brünger, A.T. (1998). Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5, 803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brünger, A.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.