메뉴 건너뛰기




Volumn 4, Issue 5, 2012, Pages 270-283

Enlightening molecular mechanisms through study of protein interactions

Author keywords

membrane fusion; molecular mechanisms; neurotransmitter release; NMR spectroscopy; protein interactions; X ray crystallography

Indexed keywords

BINDING PROTEIN; CALCIUM ION; COMPLEXIN; HETERODIMER; HOMODIMER; MULTIPROTEIN COMPLEX; MUNC13 PROTEIN; MUNC18 PROTEIN; PROTEIN RIM; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN I; SYNTAXIN 1; UNCLASSIFIED DRUG;

EID: 84867409614     PISSN: 16742788     EISSN: 17594685     Source Type: Journal    
DOI: 10.1093/jmcb/mjs036     Document Type: Review
Times cited : (23)

References (128)
  • 1
    • 0037452955 scopus 로고    scopus 로고
    • Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy
    • Arac, D., Murphy, T., and Rizo, J. (2003). Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy. Biochemistry 42, 2774-2780.
    • (2003) Biochemistry , vol.42 , pp. 2774-2780
    • Arac, D.1    Murphy, T.2    Rizo, J.3
  • 2
    • 33644804207 scopus 로고    scopus 로고
    • 2+-dependent multivalent binding of synaptotagmin-1 to phospholipids
    • Arac, D., Chen, X., Khant, H.A., et al. (2006). Close membrane-membrane proximity induced by Ca2+-dependent multivalent binding of synaptotagmin-1 to phospholipids. Nat. Struct. Mol. Biol. 13, 209-217.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 209-217
    • Arac, D.1    Chen, X.2    Khant, H.A.3
  • 3
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin, I., Rosenmund, C., Sudhof, T.C., et al. (1999). Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature 400, 457-461.
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Sudhof, T.C.3
  • 4
    • 0029808089 scopus 로고    scopus 로고
    • 2+-activated exocytosis
    • Banerjee, A., Barry, V.A., DasGupta, B.R., et al. (1996). N-ethylmaleimidesensitive factor acts at a prefusion ATP-dependent step in Ca2+-activated exocytosis. J. Biol. Chem. 271, 20223-20226.
    • (1996) J. Biol. Chem , vol.271 , pp. 20223-20226
    • Banerjee, A.1    Barry, V.A.2    Dasgupta, B.R.3
  • 5
    • 33645014145 scopus 로고    scopus 로고
    • A minimal domain responsible for Munc13 activity
    • Basu, J., Shen, N., Dulubova, I., et al. (2005). A minimal domain responsible for Munc13 activity. Nat. Struct. Mol. Biol. 12, 1017-1018.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1017-1018
    • Basu, J.1    Shen, N.2    Dulubova, I.3
  • 6
    • 33846794400 scopus 로고    scopus 로고
    • Munc13-1 C1 domain activation lowers the energy barrier for synaptic vesicle fusion
    • Basu, J., Betz, A., Brose, N., et al. (2007). Munc13-1 C1 domain activation lowers the energy barrier for synaptic vesicle fusion. J. Neurosci. 27, 1200-1210.
    • (2007) J. Neurosci , vol.27 , pp. 1200-1210
    • Basu, J.1    Betz, A.2    Brose, N.3
  • 7
    • 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
  • 8
    • 0035030935 scopus 로고    scopus 로고
    • Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming
    • Betz, A., Thakur, P., Junge, H.J., et al. (2001). Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming. Neuron 30, 183-196.
    • (2001) Neuron , vol.30 , pp. 183-196
    • Betz, A.1    Thakur, P.2    Junge, H.J.3
  • 9
    • 0037112932 scopus 로고    scopus 로고
    • Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p
    • Bracher, A., and Weissenhorn, W. (2002). Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. EMBO J. 21, 6114-6124.
    • (2002) EMBO J , vol.21 , pp. 6114-6124
    • Bracher, A.1    Weissenhorn, W.2
  • 10
    • 79961238730 scopus 로고    scopus 로고
    • Reluctance to membrane binding enables accessibility of the synaptobrevin SNARE motif for SNARE complex formation
    • Brewer, K.D., Li, W., Horne, B.E., et al. (2011). Reluctance to membrane binding enables accessibility of the synaptobrevin SNARE motif for SNARE complex formation. Proc. Natl Acad. Sci. USA 108, 12723-12728.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 12723-12728
    • Brewer, K.D.1    Li, W.2    Horne, B.E.3
  • 11
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose, N., Petrenko, A.G., Sudhof, T.C., et al. (1992). Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science 256, 1021-1025.
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Sudhof, T.C.3
  • 12
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • Brunger, A.T. (2005). Structure and function of SNARE and SNARE-interacting proteins. Q. Rev. Biophys. 38, 1-47.
    • (2005) Q. Rev. Biophys , vol.38 , pp. 1-47
    • Brunger, A.T.1
  • 13
    • 67650759736 scopus 로고    scopus 로고
    • Single-molecule studies of the neuronal SNARE fusion machinery
    • Brunger, A.T., Weninger, K., Bowen, M., et al. (2009). Single-molecule studies of the neuronal SNARE fusion machinery. Annu. Rev. Biochem. 78, 903-928.
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 903-928
    • Brunger, A.T.1    Weninger, K.2    Bowen, M.3
  • 14
    • 41949130893 scopus 로고    scopus 로고
    • Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
    • Burkhardt, P., Hattendorf, D.A., Weis, W.I., et al. (2008). Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. EMBO J. 27, 923-933.
    • (2008) EMBO J , vol.27 , pp. 923-933
    • Burkhardt, P.1    Hattendorf, D.A.2    Weis, W.I.3
  • 15
    • 34247623568 scopus 로고    scopus 로고
    • Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle
    • Cai, H., Reinisch, K., and Ferro-Novick, S. (2007). Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev. Cell 12, 671-682.
    • (2007) Dev. Cell , vol.12 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 16
    • 0028350057 scopus 로고
    • Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
    • Calakos, N., Bennett, M.K., Peterson, K.E., et al. (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
  • 17
    • 2942752010 scopus 로고    scopus 로고
    • Multiple roles for the active zone protein RIM1 alpha in late stages of neurotransmitter release
    • Calakos, N., Schoch, S., Sudhof, T.C., et al. (2004). Multiple roles for the active zone protein RIM1 alpha in late stages of neurotransmitter release. Neuron 42, 889-896.
    • (2004) Neuron , vol.42 , pp. 889-896
    • Calakos, N.1    Schoch, S.2    Sudhof, T.C.3
  • 18
    • 33745241903 scopus 로고    scopus 로고
    • The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes
    • Carpp, L.N., Ciufo, L.F., Shanks, S.G., et al. (2006). The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes. J. Cell Biol. 173, 927-936.
    • (2006) J. Cell Biol , vol.173 , pp. 927-936
    • Carpp, L.N.1    Ciufo, L.F.2    Shanks, S.G.3
  • 19
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C.M., Grote, E., Munson, M., et al. (1999). Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146, 333-344.
    • (1999) J. Cell Biol , vol.146 , pp. 333-344
    • Carr, C.M.1    Grote, E.2    Munson, M.3
  • 20
    • 0037122459 scopus 로고    scopus 로고
    • RIM1alpha is required for presynaptic long-term potentiation
    • Castillo, P.E., Schoch, S., Schmitz, F., et al. (2002). RIM1alpha is required for presynaptic long-term potentiation. Nature 415, 327-330.
    • (2002) Nature , vol.415 , pp. 327-330
    • Castillo, P.E.1    Schoch, S.2    Schmitz, F.3
  • 21
    • 0032577067 scopus 로고    scopus 로고
    • 2+-binding loop of synaptotagmin with lipid bilayers
    • Chapman, E.R., and Davis, A.F. (1998). Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers. J. Biol. Chem. 273, 13995-14001.
    • (1998) J. Biol. Chem , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 22
    • 33750448672 scopus 로고    scopus 로고
    • Capturing protein-protein complexes at equilibrium: The holdup comparative chromatographic retention assay
    • Charbonnier, S., Zanier, K., Masson, M., et al. (2006). Capturing protein-protein complexes at equilibrium: the holdup comparative chromatographic retention assay. Protein Expr. Purif. 50, 89-101.
    • (2006) Protein Expr. Purif , vol.50 , pp. 89-101
    • Charbonnier, S.1    Zanier, K.2    Masson, M.3
  • 23
    • 0037204076 scopus 로고    scopus 로고
    • Three-dimensional structure of the complexin/SNARE complex
    • Chen, X., Tomchick, D.R., Kovrigin, E., et al. (2002). Three-dimensional structure of the complexin/SNARE complex. Neuron 33, 397-409.
    • (2002) Neuron , vol.33 , pp. 397-409
    • Chen, X.1    Tomchick, D.R.2    Kovrigin, E.3
  • 24
    • 77949264921 scopus 로고    scopus 로고
    • Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex
    • Choi, U.B., Strop, P., Vrljic, M., et al. (2010). Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex. Nat. Struct. Mol. Biol. 17, 318-324.
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 318-324
    • Choi, U.B.1    Strop, P.2    Vrljic, M.3
  • 25
    • 4344616380 scopus 로고    scopus 로고
    • 2+ binding to synaptotagmin 4
    • Dai, H., Shin, O.H., Machius, M., et al. (2004). Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4. Nat. Struct. Mol. Biol. 11, 844-849.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 844-849
    • Dai, H.1    Shin, O.H.2    MacHius, M.3
  • 26
    • 26644474099 scopus 로고    scopus 로고
    • Crystal structure of the RIM2 C2A-domain at 1 A resolution
    • Dai, H., Tomchick, D.R., Garcia, J., et al. (2005). Crystal structure of the RIM2 C2A-domain at 1. A resolution. Biochemistry 44, 13533-13542.
    • (2005) Biochemistry , vol.44 , pp. 13533-13542
    • Dai, H.1    Tomchick, D.R.2    Garcia, J.3
  • 27
    • 33847269603 scopus 로고    scopus 로고
    • 2+-phospholipid complex in neurotransmitter release
    • Dai, H., Shen, N., Arac, D., et al. (2007). A quaternary SNAREsynaptotagmin- Ca2+-phospholipid complex in neurotransmitter release. J. Mol. Biol. 367, 848-863.
    • (2007) J. Mol. Biol , vol.367 , pp. 848-863
    • Dai, H.1    Shen, N.2    Arac, D.3
  • 28
    • 64749107397 scopus 로고    scopus 로고
    • Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming
    • Deak, F., Xu, Y., Chang, W.P., et al. (2009). Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming. J. Cell Biol. 184, 751-764.
    • (2009) J. Cell Biol , vol.184 , pp. 751-764
    • Deak, F.1    Xu, Y.2    Chang, W.P.3
  • 29
    • 78651504517 scopus 로고    scopus 로고
    • RIM proteins activate vesicle priming by reversing autoinhibitory homodimerization of Munc13
    • Deng, L., Kaeser, P.S., Xu, W., et al. (2011). RIM proteins activate vesicle priming by reversing autoinhibitory homodimerization of Munc13. Neuron 69, 317-331.
    • (2011) Neuron , vol.69 , pp. 317-331
    • Deng, L.1    Kaeser, P.S.2    Xu, W.3
  • 30
    • 0027180569 scopus 로고
    • Synaptic transmission persists in synaptotagmin mutants of Drosophila
    • DiAntonio, A., Parfitt, K.D., and Schwarz, T.L. (1993). Synaptic transmission persists in synaptotagmin mutants of Drosophila. Cell 73, 1281-1290.
    • (1993) Cell , vol.73 , pp. 1281-1290
    • Diantonio, A.1    Parfitt, K.D.2    Schwarz, T.L.3
  • 31
    • 0033575749 scopus 로고    scopus 로고
    • A conformational switch in syntaxin during exocytosis: Role of munc18
    • Dulubova, I., Sugita, S., Hill, S., et al. (1999). A conformational switch in syntaxin during exocytosis: role of munc18. EMBO J. 18, 4372-4382.
    • (1999) EMBO J , vol.18 , pp. 4372-4382
    • Dulubova, I.1    Sugita, S.2    Hill, S.3
  • 32
    • 0035126830 scopus 로고    scopus 로고
    • Vam3p structure reveals conserved and divergent properties of syntaxins
    • Dulubova, I., Yamaguchi, T., Wang, Y., et al. (2001). Vam3p structure reveals conserved and divergent properties of syntaxins. Nat. Struct. Biol. 8, 258-264.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 258-264
    • Dulubova, I.1    Yamaguchi, T.2    Wang, Y.3
  • 33
    • 0037099492 scopus 로고    scopus 로고
    • How Tlg2p/syntaxin 16 'snares' Vps45
    • Dulubova, I., Yamaguchi, T., Gao, Y., et al. (2002). How Tlg2p/syntaxin 16 'snares' Vps45. EMBO J. 21, 3620-3631.
    • (2002) EMBO J , vol.21 , pp. 3620-3631
    • Dulubova, I.1    Yamaguchi, T.2    Gao, Y.3
  • 34
    • 28844449520 scopus 로고    scopus 로고
    • A Munc13/RIM/Rab3 tripartite complex: From priming to plasticity?
    • Dulubova, I., Lou, X., Lu, J., et al. (2005). A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity? EMBO J. 24, 2839-2850.
    • (2005) EMBO J , vol.24 , pp. 2839-2850
    • Dulubova, I.1    Lou, X.2    Lu, J.3
  • 35
    • 33847326814 scopus 로고    scopus 로고
    • Munc18-1 binds directly to the neuronal SNARE complex
    • Dulubova, I., Khvotchev, M., Liu, S., et al. (2007). Munc18-1 binds directly to the neuronal SNARE complex. Proc. Natl Acad. Sci. USA 104, 2697-2702.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2697-2702
    • Dulubova, I.1    Khvotchev, M.2    Liu, S.3
  • 36
    • 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., et al. (1997). Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem. 272, 28036-28041.
    • (1997) J. Biol. Chem , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3
  • 37
    • 0032544441 scopus 로고    scopus 로고
    • Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A
    • Fernandez, I., Ubach, J., Dulubova, I., et al. (1998). Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A. Cell 94, 841-849.
    • (1998) Cell , vol.94 , pp. 841-849
    • Fernandez, I.1    Ubach, J.2    Dulubova, I.3
  • 38
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin 1 C2b-domain Synaptotagmin 1 as a phospholipid binding machine
    • Fernandez, I., Arac, D., Ubach, J., et al. (2001). Three-dimensional structure of the synaptotagmin 1 C2b-domain. Synaptotagmin 1 as a phospholipid binding machine. Neuron 32, 1057-1069.
    • (2001) Neuron , vol.32 , pp. 1057-1069
    • Fernandez, I.1    Arac, D.2    Ubach, J.3
  • 39
    • 0035282457 scopus 로고    scopus 로고
    • Synaptotagmin i functions as a calcium regulator of release probability
    • Fernandez-Chacon, R., Konigstorfer, A., Gerber, S.H., et al. (2001). Synaptotagmin I functions as a calcium regulator of release probability. Nature 410, 41-49.
    • (2001) Nature , vol.410 , pp. 41-49
    • Fernandez-Chacon, R.1    Konigstorfer, A.2    Gerber, S.H.3
  • 40
    • 0036813665 scopus 로고    scopus 로고
    • 2+ binding to the C2A domain of synaptotagmin 1
    • Fernandez-Chacon, R., Shin, O.H., Konigstorfer, A., et al. (2002). Structure/ function analysis of Ca2+ binding to the C2A domain of synaptotagmin 1. J. Neurosci. 22, 8438-8446.
    • (2002) J. Neurosci , vol.22 , pp. 8438-8446
    • Fernandez-Chacon, R.1    Shin, O.H.2    Konigstorfer, A.3
  • 41
    • 0032959242 scopus 로고    scopus 로고
    • Folding intermediates of SNARE complex assembly
    • Fiebig, K.M., Rice, L.M., Pollock, E., et al. (1999). Folding intermediates of SNARE complex assembly. Nat. Struct. Biol. 6, 117-123.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 117-123
    • Fiebig, K.M.1    Rice, L.M.2    Pollock, E.3
  • 42
    • 0037401513 scopus 로고    scopus 로고
    • 2+-activated K+ channel revealed by coimmunoprecipitation and pull-down assays: Implications for identification of protein-protein interactions
    • Fletcher, S., Bowden, S.E., and Marrion, N.V. (2003). False interaction of syntaxin 1A with a Ca2+-activated K+ channel revealed by coimmunoprecipitation and pull-down assays: implications for identification of protein-protein interactions. Neuropharmacology 44, 817-827.
    • (2003) Neuropharmacology , vol.44 , pp. 817-827
    • Fletcher, S.1    Bowden, S.E.2    Marrion, N.V.3
  • 43
    • 70149094784 scopus 로고    scopus 로고
    • The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p
    • Furgason, M.L., MacDonald, C., Shanks, S.G., et al. (2009). The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p. Proc. Natl Acad. Sci. USA 106, 14303-14308.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14303-14308
    • Furgason, M.L.1    MacDonald, C.2    Shanks, S.G.3
  • 44
    • 0842269784 scopus 로고    scopus 로고
    • A conformational switch in the Piccolo C2A domain regulated by alternative splicing
    • Garcia, J., Gerber, S.H., Sugita, S., et al. (2004). A conformational switch in the Piccolo C2A domain regulated by alternative splicing. Nat. Struct. Mol. Biol. 11, 45-53.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 45-53
    • Garcia, J.1    Gerber, S.H.2    Sugita, S.3
  • 45
    • 0031595590 scopus 로고    scopus 로고
    • 15N multidimensional NMR to study the structure and dynamics of proteins
    • Gardner, K.H., and Kay, L.E. (1998). The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27, 357-406.
    • (1998) Annu. Rev. Biophys. Biomol. Struct , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 46
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
    • Gelis, I., Bonvin, A.M., Keramisanou, D., et al. (2007). Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell 131, 756-769.
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.2    Keramisanou, D.3
  • 47
    • 0028061861 scopus 로고
    • 2+ sensor for transmitter release at a central synapse
    • Geppert, M., Goda, Y., Hammer, R.E., et al. (1994). Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse. Cell 79, 717-727.
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Hammer, R.E.3
  • 48
    • 0035794636 scopus 로고    scopus 로고
    • 2+ regulation of neurotransmitter release
    • Gerber, S.H., Garcia, J., Rizo, J., et al. (2001). An unusual C2-domain in the active-zone protein piccolo: implications for Ca2+ regulation of neurotransmitter release. EMBO J. 20, 1605-1619.
    • (2001) EMBO J , vol.20 , pp. 1605-1619
    • Gerber, S.H.1    Garcia, J.2    Rizo, J.3
  • 49
    • 51749100843 scopus 로고    scopus 로고
    • Conformational switch of syntaxin-1 controls synaptic vesicle fusion
    • Gerber, S.H., Rah, J.C., Min, S.W., et al. (2008). Conformational switch of syntaxin-1 controls synaptic vesicle fusion. Science 321, 1507-1510.
    • (2008) Science , vol.321 , pp. 1507-1510
    • Gerber, S.H.1    Rah, J.C.2    Min, S.W.3
  • 50
    • 58849105859 scopus 로고    scopus 로고
    • Alternative zippering as an on-off switch for SNARE-mediated fusion
    • Giraudo, C.G., Garcia-Diaz, A., Eng, W.S., et al. (2009). Alternative zippering as an on-off switch for SNARE-mediated fusion. Science 323, 512-516.
    • (2009) Science , vol.323 , pp. 512-516
    • Giraudo, C.G.1    Garcia-Diaz, A.2    Eng, W.S.3
  • 51
    • 34547738934 scopus 로고    scopus 로고
    • Crystal structure of the RIM1alpha C2B domain at 1 A resolution
    • Guan, R., Dai, H., Tomchick, D.R., et al. (2007). Crystal structure of the RIM1alpha C2B domain at 1. A resolution. Biochemistry 46, 8988-8998.
    • (2007) Biochemistry , vol.46 , pp. 8988-8998
    • Guan, R.1    Dai, H.2    Tomchick, D.R.3
  • 52
    • 38949089701 scopus 로고    scopus 로고
    • Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes
    • Guan, R., Dai, H., and Rizo, J. (2008). Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes. Biochemistry 47, 1474-1481.
    • (2008) Biochemistry , vol.47 , pp. 1474-1481
    • Guan, R.1    Dai, H.2    Rizo, J.3
  • 53
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quickfreeze/ deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., et al. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quickfreeze/ 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
  • 54
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S.M., Neil, L.C., and Gardner, K.H. (2003). Structural basis of a phototropin light switch. Science 301, 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 55
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C.A., and Sudhof, T.C. (1993). Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366, 347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Sudhof, T.C.3
  • 56
    • 0344289516 scopus 로고    scopus 로고
    • NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
    • Hazzard, J., Sudhof, T.C., and Rizo, J. (1999). NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin. J. Biomol. NMR 14, 203-207.
    • (1999) J. Biomol. NMR , vol.14 , pp. 203-207
    • Hazzard, J.1    Sudhof, T.C.2    Rizo, J.3
  • 57
    • 34748846347 scopus 로고    scopus 로고
    • A complexin fusion clamp regulates spontaneous neurotransmitter release and synaptic growth
    • Huntwork, S., and Littleton, J.T. (2007). A complexin fusion clamp regulates spontaneous neurotransmitter release and synaptic growth. Nat. Neurosci. 10, 1235-1237.
    • (2007) Nat. Neurosci , vol.10 , pp. 1235-1237
    • Huntwork, S.1    Littleton, J.T.2
  • 58
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs-engines for membrane fusion
    • Jahn, R., and Scheller, R.H. (2006). SNAREs-engines for membrane fusion. Nat. Rev. Mol. Cell Biol. 7, 631-643.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 59
    • 4043075637 scopus 로고    scopus 로고
    • 2+ sensor/effector complex that controls short-term synaptic plasticity
    • Junge, H.J., Rhee, J.S., Jahn, O., et al. (2004). Calmodulin and Munc13 form a Ca2+ sensor/effector complex that controls short-term synaptic plasticity. Cell 118, 389-401.
    • (2004) Cell , vol.118 , pp. 389-401
    • Junge, H.J.1    Rhee, J.S.2    Jahn, O.3
  • 60
    • 78651509693 scopus 로고    scopus 로고
    • 2+ channels to presynaptic active zones via a direct PDZ-domain interaction
    • Kaeser, P.S., Deng, L., Wang, Y., et al. (2011). RIM proteins tether Ca2+ channels to presynaptic active zones via a direct PDZ-domain interaction. Cell 144, 282-295.
    • (2011) Cell , vol.144 , pp. 282-295
    • Kaeser, P.S.1    Deng, L.2    Wang, Y.3
  • 61
    • 36049049393 scopus 로고    scopus 로고
    • Dual modes of Munc18-1/ SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminus
    • Khvotchev, M., Dulubova, I., Sun, J., et al. (2007). Dual modes of Munc18-1/ SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminus. J. Neurosci. 27, 12147-12155.
    • (2007) J. Neurosci , vol.27 , pp. 12147-12155
    • Khvotchev, M.1    Dulubova, I.2    Sun, J.3
  • 62
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim, A.S., Kakalis, L.T., Abdul-Manan, N., et al. (2000). Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404, 151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3
  • 63
    • 0034810799 scopus 로고    scopus 로고
    • A post-docking role for active zone protein Rim
    • Koushika, S.P., Richmond, J.E., Hadwiger, G., et al. (2001). A post-docking role for active zone protein Rim. Nat. Neurosci. 4, 997-1005.
    • (2001) Nat. Neurosci , vol.4 , pp. 997-1005
    • Koushika, S.P.1    Richmond, J.E.2    Hadwiger, G.3
  • 64
    • 0038455923 scopus 로고    scopus 로고
    • NMR analysis of methyl groups at 100-500 kDa: Model systems and Arp2/3 complex
    • Kreishman-Deitrick, M., Egile, C., Hoyt, D.W., et al. (2003). NMR analysis of methyl groups at 100-500 kDa: model systems and Arp2/3 complex. Biochemistry 42, 8579-8586.
    • (2003) Biochemistry , vol.42 , pp. 8579-8586
    • Kreishman-Deitrick, M.1    Egile, C.2    Hoyt, D.W.3
  • 65
    • 79961024212 scopus 로고    scopus 로고
    • Complexin crosslinks prefusion SNAREs into a zigzag array
    • Kummel, D., Krishnakumar, S.S., Radoff, D.T., et al. (2011). Complexin crosslinks prefusion SNAREs into a zigzag array. Nat. Struct. Mol. Biol. 18, 927-933.
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 927-933
    • Kummel, D.1    Krishnakumar, S.S.2    Radoff, D.T.3
  • 66
    • 33748568111 scopus 로고    scopus 로고
    • Molecular dissection of the Munc18c/syntaxin4 interaction: Implications for regulation of membrane trafficking
    • Latham, C.F., Lopez, J.A., Hu, S.H., et al. (2006). Molecular dissection of the Munc18c/syntaxin4 interaction: implications for regulation of membrane trafficking. Traffic 7, 1408-1419.
    • (2006) Traffic , vol.7 , pp. 1408-1419
    • Latham, C.F.1    Lopez, J.A.2    Hu, S.H.3
  • 67
    • 80054056038 scopus 로고    scopus 로고
    • The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors
    • Li, W., Ma, C., Guan, R., et al. (2011). The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors. Structure 19, 1443-1455.
    • (2011) Structure , vol.19 , pp. 1443-1455
    • Li, W.1    Ma, C.2    Guan, R.3
  • 68
    • 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
  • 69
    • 0027438591 scopus 로고
    • 2+- activated neurotransmitter release
    • Littleton, J.T., Stern, M., Schulze, K., et al. (1993). Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in Ca2+- activated neurotransmitter release. Cell 74, 1125-1134.
    • (1993) Cell , vol.74 , pp. 1125-1134
    • Littleton, J.T.1    Stern, M.2    Schulze, K.3
  • 70
    • 33745878240 scopus 로고    scopus 로고
    • Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch
    • Lu, J., Machius, M., Dulubova, I., et al. (2006). Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch. PLoS Biol. 4, e192.
    • (2006) PLoS Biol , vol.4
    • Lu, J.1    MacHius, M.2    Dulubova, I.3
  • 71
    • 77949330731 scopus 로고    scopus 로고
    • Accessory alpha-helix of complexin i can displace VAMP2 locally in the complexin-SNARE quaternary complex
    • Lu, B., Song, S., and Shin, Y.K. (2010). Accessory alpha-helix of complexin I can displace VAMP2 locally in the complexin-SNARE quaternary complex. J. Mol. Biol. 396, 602-609.
    • (2010) J. Mol. Biol , vol.396 , pp. 602-609
    • Lu, B.1    Song, S.2    Shin, Y.K.3
  • 72
    • 85027945821 scopus 로고    scopus 로고
    • Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex
    • Ma, C., Li, W., Xu, Y., et al. (2011). Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex. Nat. Struct. Mol. Biol. 18, 542-549.
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 542-549
    • Ma, C.1    Li, W.2    Xu, Y.3
  • 73
    • 0037130255 scopus 로고    scopus 로고
    • 2+-binding motif of synaptotagmin is required for synaptic transmission in vivo
    • Mackler, J.M., Drummond, J.A., Loewen, C.A., et al. (2002). The C2B Ca2+-binding motif of synaptotagmin is required for synaptic transmission in vivo. Nature 418, 340-344.
    • (2002) Nature , vol.418 , pp. 340-344
    • MacKler, J.M.1    Drummond, J.A.2    Loewen, C.A.3
  • 74
    • 58849164361 scopus 로고    scopus 로고
    • Complexin controls the force transfer from SNARE complexes to membranes in fusion
    • Maximov, A., Tang, J., Yang, X., et al. (2009). Complexin controls the force transfer from SNARE complexes to membranes in fusion. Science 323, 516-521.
    • (2009) Science , vol.323 , pp. 516-521
    • Maximov, A.1    Tang, J.2    Yang, X.3
  • 75
    • 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., and Haas, A. (1996). Sec18p (NSF)-driven release of Sec17p (alpha-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
  • 76
    • 55549102680 scopus 로고    scopus 로고
    • UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin
    • McEwen, J.M., and Kaplan, J.M. (2008). UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin. Mol. Biol. Cell 19, 3836-3846.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3836-3846
    • McEwen, J.M.1    Kaplan, J.M.2
  • 77
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon, H.T., Missler, M., Li, C., et al. (1995). Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 83, 111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3
  • 78
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • Misura, K.M., Scheller, R.H., and Weis, W.I. (2000). Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature 404, 355-362.
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 79
    • 0031709722 scopus 로고    scopus 로고
    • Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p
    • Nicholson, K.L., Munson, M., Miller, R.B., et al. (1998). Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nat. Struct. Biol. 5, 793-802.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 793-802
    • Nicholson, K.L.1    Munson, M.2    Miller, R.B.3
  • 80
    • 4744344106 scopus 로고    scopus 로고
    • 2+-dependent neurotransmitter release
    • Nishiki, T., and Augustine, G.J. (2004). Dual roles of the C2B domain of synaptotagmin I in synchronizing Ca2+-dependent neurotransmitter release. J. Neurosci. 24, 8542-8550.
    • (2004) J. Neurosci , vol.24 , pp. 8542-8550
    • Nishiki, T.1    Augustine, G.J.2
  • 81
    • 0027319325 scopus 로고
    • Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin
    • Nonet, M.L., Grundahl, K., Meyer, B.J., et al. (1993). Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin. Cell 73, 1291-1305.
    • (1993) Cell , vol.73 , pp. 1291-1305
    • Nonet, M.L.1    Grundahl, K.2    Meyer, B.J.3
  • 82
    • 77952915958 scopus 로고    scopus 로고
    • Protein NMR using paramagnetic ions
    • Otting, G. (2010). Protein NMR using paramagnetic ions. Annu. Rev. Biophys. 39, 387-405.
    • (2010) Annu. Rev. Biophys , vol.39 , pp. 387-405
    • Otting, G.1
  • 83
    • 0034733545 scopus 로고    scopus 로고
    • Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions
    • Pabst, S., Hazzard, J.W., Antonin, W., et al. (2000). Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. J. Biol. Chem. 275, 19808-19818.
    • (2000) J. Biol. Chem , vol.275 , pp. 19808-19818
    • Pabst, S.1    Hazzard, J.W.2    Antonin, W.3
  • 84
    • 67651160303 scopus 로고    scopus 로고
    • Remote homology between Munc13 MUN domain and vesicle tethering complexes
    • Pei, J., Ma, C., Rizo, J., et al. (2009). Remote homology between Munc13 MUN domain and vesicle tethering complexes. J. Mol. Biol. 391, 509-517.
    • (2009) J. Mol. Biol , vol.391 , pp. 509-517
    • Pei, J.1    Ma, C.2    Rizo, J.3
  • 85
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin, M.S., Fried, V.A., Mignery, G.A., et al. (1990). Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345, 260-263.
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3
  • 86
    • 0031668972 scopus 로고    scopus 로고
    • The synaptic SNARE complex is a parallel four-stranded helical bundle
    • Poirier, M.A., Xiao,W., Macosko, J.C., et al. (1998). The synaptic SNARE complex is a parallel four-stranded helical bundle. Nat. Struct. Biol. 5, 765-769.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 765-769
    • Poirier, M.A.1    Xiao, W.2    Macosko, J.C.3
  • 87
    • 78651078463 scopus 로고    scopus 로고
    • Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex
    • Rathore, S.S., Bend, E.G., Yu, H., et al. (2010). Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex. Proc. Natl Acad. Sci. USA 107, 22399-22406.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 22399-22406
    • Rathore, S.S.1    Bend, E.G.2    Yu, H.3
  • 88
    • 0035846908 scopus 로고    scopus 로고
    • 2+-dependent neurotransmitter release
    • Reim, K., Mansour, M., Varoqueaux, F., et al. (2001). Complexins regulate a late step in Ca2+-dependent neurotransmitter release. Cell 104, 71-81.
    • (2001) Cell , vol.104 , pp. 71-81
    • Reim, K.1    Mansour, M.2    Varoqueaux, F.3
  • 89
    • 18244389735 scopus 로고    scopus 로고
    • Beta phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc13s and not by PKCs
    • Rhee, J.S., Betz, A., Pyott, S., et al. (2002). Beta phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc13s and not by PKCs. Cell 108, 121-133.
    • (2002) Cell , vol.108 , pp. 121-133
    • Rhee, J.S.1    Betz, A.2    Pyott, S.3
  • 90
    • 29444436513 scopus 로고    scopus 로고
    • 2+ affinity of synaptotagmin 1
    • Rhee, J.S., Li, L.Y., Shin, O.H., et al. (2005). Augmenting neurotransmitter release by enhancing the apparent Ca2+ affinity of synaptotagmin 1. Proc. Natl Acad. Sci. USA 102, 18664-18669.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18664-18669
    • Rhee, J.S.1    Li, L.Y.2    Shin, O.H.3
  • 91
    • 0033349884 scopus 로고    scopus 로고
    • UNC-13 is required for synaptic vesicle fusion in C. elegans
    • Richmond, J.E., Davis, W.S., and Jorgensen, E.M. (1999). UNC-13 is required for synaptic vesicle fusion in C. elegans. Nat. Neurosci. 2, 959-964.
    • (1999) Nat. Neurosci , vol.2 , pp. 959-964
    • Richmond, J.E.1    Davis, W.S.2    Jorgensen, E.M.3
  • 92
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond, J.E., Weimer, R.M., and Jorgensen, E.M. (2001). An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature 412, 338-341.
    • (2001) Nature , vol.412 , pp. 338-341
    • Richmond, J.E.1    Weimer, R.M.2    Jorgensen, E.M.3
  • 93
    • 0037120882 scopus 로고    scopus 로고
    • Solution NMR techniques for large molecular and supramolecular structures
    • Riek, R., Fiaux, J., Bertelsen, E.B., et al. (2002). Solution NMR techniques for large molecular and supramolecular structures. J. Am. Chem. Soc. 124, 12144-12153.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 12144-12153
    • Riek, R.1    Fiaux, J.2    Bertelsen, E.B.3
  • 94
    • 0032568662 scopus 로고    scopus 로고
    • 2+-binding domain
    • Rizo, J., and Sudhof, T.C. (1998). C2-domains, structure and function of a universal Ca2+-binding domain. J. Biol. Chem. 273, 15879-15882.
    • (1998) J. Biol. Chem , vol.273 , pp. 15879-15882
    • Rizo, J.1    Sudhof, T.C.2
  • 96
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • Rizo, J., Chen, X., and Arac, D. (2006). Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trends Cell Biol. 16, 339-350.
    • (2006) Trends Cell Biol , vol.16 , pp. 339-350
    • Rizo, J.1    Chen, X.2    Arac, D.3
  • 97
    • 0037130260 scopus 로고    scopus 로고
    • 2+ binding in the C2A domain
    • Robinson, I.M., Ranjan, R., and Schwarz, T.L. (2002). Synaptotagmins I and IV promote transmitter release independently of Ca2+ binding in the C2A domain. Nature 418, 336-340.
    • (2002) Nature , vol.418 , pp. 336-340
    • Robinson, I.M.1    Ranjan, R.2    Schwarz, T.L.3
  • 98
    • 0030589148 scopus 로고    scopus 로고
    • Selective methyl group protonation of perdeuterated proteins
    • Rosen, M.K., Gardner, K.H., Willis, R.C., et al. (1996). Selective methyl group protonation of perdeuterated proteins. J. Mol. Biol. 263, 627-636.
    • (1996) J. Mol. Biol , vol.263 , pp. 627-636
    • Rosen, M.K.1    Gardner, K.H.2    Willis, R.C.3
  • 99
    • 77649179384 scopus 로고    scopus 로고
    • Methyl groups as probes of supramolecular structure, dynamics and function
    • Ruschak, A.M., and Kay, L.E. (2010). Methyl groups as probes of supramolecular structure, dynamics and function. J. Biomol. NMR 46, 75-87.
    • (2010) J. Biomol. NMR , vol.46 , pp. 75-87
    • Ruschak, A.M.1    Kay, L.E.2
  • 100
    • 0037122458 scopus 로고    scopus 로고
    • RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone
    • Schoch, S., Castillo, P.E., Jo, T., et al. (2002). RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone. Nature 415, 321-326.
    • (2002) Nature , vol.415 , pp. 321-326
    • Schoch, S.1    Castillo, P.E.2    Jo, T.3
  • 101
    • 0029666292 scopus 로고    scopus 로고
    • 2+-bindingmotif in C2 domains of synaptotagmin and protein kinase C
    • Shao, X., Davletov, B.A., Sutton, R.B., et al. (1996). Bipartite Ca2+-bindingmotif in C2 domains of synaptotagmin and protein kinase C. Science 273, 248-251.
    • (1996) Science , vol.273 , pp. 248-251
    • Shao, X.1    Davletov, B.A.2    Sutton, R.B.3
  • 102
    • 0031019191 scopus 로고    scopus 로고
    • 2+-dependent electrostatic switch
    • Shao, X., Li, C., Fernandez, I., et al. (1997). Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch. Neuron 18, 133-142.
    • (1997) Neuron , vol.18 , pp. 133-142
    • Shao, X.1    Li, C.2    Fernandez, I.3
  • 103
    • 0032541943 scopus 로고    scopus 로고
    • 2+ induce a conformational change?
    • Shao, X., Fernandez, I., Sudhof, T.C., et al. (1998). Solution structures of the Ca2+-free and Ca2+-bound C2A domain of synaptotagmin I: does Ca2+ induce a conformational change? Biochemistry 37, 16106-16115.
    • (1998) Biochemistry , vol.37 , pp. 16106-16115
    • Shao, X.1    Fernandez, I.2    Sudhof, T.C.3
  • 104
    • 33845987734 scopus 로고    scopus 로고
    • Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
    • Shen, J., Tareste, D.C., Paumet, F., et al. (2007). Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. Cell 128, 183-195.
    • (2007) Cell , vol.128 , pp. 183-195
    • Shen, J.1    Tareste, D.C.2    Paumet, F.3
  • 105
    • 77954715092 scopus 로고    scopus 로고
    • SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion
    • Shen, J., Rathore, S.S., Khandan, L., et al. (2010). SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion. J. Cell Biol. 190, 55-63.
    • (2010) J. Cell Biol , vol.190 , pp. 55-63
    • Shen, J.1    Rathore, S.S.2    Khandan, L.3
  • 106
    • 77949266565 scopus 로고    scopus 로고
    • 2+ regulator of synaptic exocytosis
    • Shin, O.H., Lu, J., Rhee, J.S., et al. (2010). Munc13 C2B domain-an activitydependent Ca2+ regulator of synaptic exocytosis. Nat. Struct. Mol. Biol. 17, 280-288.
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 280-288
    • Shin, O.H.1    Lu, J.2    Rhee, J.S.3
  • 107
    • 0027517462 scopus 로고
    • A protein assemblydisassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., Bennett, M.K., Whiteheart, S.W., et al. (1993a). A protein assemblydisassembly 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
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3
  • 108
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Sollner, T., Whiteheart, S.W., Brunner, M., et al. (1993b). SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324.
    • (1993) Nature , vol.362 , pp. 318-324
    • Sollner, T.1    Whiteheart, S.W.2    Brunner, M.3
  • 109
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers, R., and Kay, L.E. (2007). Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445, 618-622.
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 110
    • 33646128965 scopus 로고    scopus 로고
    • Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
    • Stroupe, C., Collins, K.M., Fratti, R.A., et al. (2006). Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J. 25, 1579-1589.
    • (2006) EMBO J , vol.25 , pp. 1579-1589
    • Stroupe, C.1    Collins, K.M.2    Fratti, R.A.3
  • 111
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T.C. (2004). The synaptic vesicle cycle. Annu. Rev.Neurosci. 27, 509-547.
    • (2004) Annu. Rev.Neurosci , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 112
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • Sudhof, T.C., and Rothman, J.E. (2009). Membrane fusion: grappling with SNARE and SM proteins. Science 323, 474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 113
    • 0028986240 scopus 로고
    • 2+ / phospholipid-binding fold
    • Sutton, R.B., Davletov, B.A., Berghuis, A.M., et al. (1995). Structure of the first C2 domain of synaptotagmin I: a novel Ca2+ /phospholipid-binding fold. Cell 80, 929-938.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3
  • 114
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2 A resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R., et al. (1998). Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. A resolution. Nature 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3
  • 115
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang, J., Maximov, A., Shin, O.H., et al. (2006). A complexin/ synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126, 1175-1187.
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3
  • 116
    • 0032527312 scopus 로고    scopus 로고
    • 2+ions bind to the tip of a C2-domain?
    • Ubach, J., Zhang, X., Shao, X., et al. (1998). Ca2+ binding to synaptotagmin: how many Ca2+ ions bind to the tip of a C2-domain? EMBO J. 17, 3921-3930.
    • (1998) EMBO J , vol.17 , pp. 3921-3930
    • Ubach, J.1    Zhang, X.2    Shao, X.3
  • 117
    • 0033143316 scopus 로고    scopus 로고
    • Structure of the Janus-faced C2B domain of rabphilin
    • Ubach, J., Garcia, J., Nittler, M.P., et al. (1999). Structure of the Janus-faced C2B domain of rabphilin. Nat. Cell Biol. 1, 106-112.
    • (1999) Nat. Cell Biol , vol.1 , pp. 106-112
    • Ubach, J.1    Garcia, J.2    Nittler, M.P.3
  • 118
    • 0035918350 scopus 로고    scopus 로고
    • 2+-binding module
    • Ubach, J., Lao, Y., Fernandez, I., et al. (2001). The C2B domain of synaptotagmin I is a Ca2+-binding module. Biochemistry 40, 5854-5860.
    • (2001) Biochemistry , vol.40 , pp. 5854-5860
    • Ubach, J.1    Lao, Y.2    Fernandez, I.3
  • 119
    • 0034603030 scopus 로고    scopus 로고
    • Synaptic assembly of the brain in the absence of neurotransmitter secretion
    • Verhage, M., Maia, A.S., Plomp, J.J., et al. (2000). Synaptic assembly of the brain in the absence of neurotransmitter secretion. Science 287, 864-869.
    • (2000) Science , vol.287 , pp. 864-869
    • Verhage, M.1    Maia, A.S.2    Plomp, J.J.3
  • 120
    • 38949211822 scopus 로고    scopus 로고
    • Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex
    • Weninger, K., Bowen, M.E., Choi, U.B., et al. (2008). Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16, 308-320.
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3
  • 121
    • 77749298991 scopus 로고    scopus 로고
    • Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle
    • Xu, Y., Su, L., and Rizo, J. (2010). Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle. Biochemistry 49, 1568-1576.
    • (2010) Biochemistry , vol.49 , pp. 1568-1576
    • Xu, Y.1    Su, L.2    Rizo, J.3
  • 122
    • 34948901461 scopus 로고    scopus 로고
    • Distinct domains of complexin i differentially regulate neurotransmitter release
    • Xue, M., Reim, K., Chen, X., et al. (2007). Distinct domains of complexin I differentially regulate neurotransmitter release. Nat. Struct. Mol. Biol. 14, 949-958.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 949-958
    • Xue, M.1    Reim, K.2    Chen, X.3
  • 123
    • 55549100557 scopus 로고    scopus 로고
    • The Janus-faced nature of the C2B domain is fundamental for synaptotagmin-1 function
    • Xue, M., Ma, C., Craig, T.K., et al. (2008). The Janus-faced nature of the C2B domain is fundamental for synaptotagmin-1 function. Nat. Struct. Mol. Biol. 15, 1160-1168.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 1160-1168
    • Xue, M.1    Ma, C.2    Craig, T.K.3
  • 124
    • 77951975523 scopus 로고    scopus 로고
    • Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity
    • Xue, M., Craig, T.K., Xu, J., et al. (2010). Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity. Nat. Struct. Mol. Biol. 17, 568-575.
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 568-575
    • Xue, M.1    Craig, T.K.2    Xu, J.3
  • 125
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi, T., Dulubova, I., Min, S.W., et al. (2002). Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev. Cell 2, 295-305.
    • (2002) Dev. Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3
  • 126
    • 0034707644 scopus 로고    scopus 로고
    • Nsec1 binds a closed conformation of syntaxin1A
    • Yang, B., Steegmaier, M., Gonzalez, L.C., Jr., et al. (2000). nSec1 binds a closed conformation of syntaxin1A. J. Cell Biol. 148, 247-252.
    • (2000) J. Cell Biol , vol.148 , pp. 247-252
    • Yang, B.1    Steegmaier, M.2    Gonzalez Jr., L.C.3
  • 127
    • 78649930845 scopus 로고    scopus 로고
    • 2+sensor via its accessory alpha helix
    • Yang, X., Kaeser-Woo, Y.J., Pang, Z.P., et al. (2010). Complexin clamps asynchronous release by blocking a secondary Ca2+ sensor via its accessory alpha helix. Neuron 68, 907-920.
    • (2010) Neuron , vol.68 , pp. 907-920
    • Yang, X.1    Kaeser-Woo, Y.J.2    Pang, Z.P.3
  • 128
    • 0032497406 scopus 로고    scopus 로고
    • 2A-domain of synaptotagmin i
    • Zhang, X., Rizo, J., and Sudhof, T.C. (1998). Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry 37, 12395-12403.
    • (1998) Biochemistry , vol.37 , pp. 12395-12403
    • Zhang, X.1    Rizo, J.2    Sudhof, T.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.