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Volumn 138, Issue 5, 2009, Pages 935-946

Synaptotagmin-1 Docks Secretory Vesicles to Syntaxin-1/SNAP-25 Acceptor Complexes

Author keywords

CELLBIO; MOLNEURO

Indexed keywords

MUNC18 PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN I; SYNTAXIN 1;

EID: 69449108209     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2009.07.027     Document Type: Article
Times cited : (228)

References (58)
  • 2
    • 33745029549 scopus 로고    scopus 로고
    • Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion
    • Bhalla A., Chicka M.C., Tucker W.C., and Chapman E.R. Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion. Nat. Struct. Mol. Biol. 13 (2006) 323-330
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 323-330
    • Bhalla, A.1    Chicka, M.C.2    Tucker, W.C.3    Chapman, E.R.4
  • 4
    • 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. Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila. Neuron 15 (1995) 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
  • 5
    • 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., and Fasshauer D. Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. EMBO J. 27 (2008) 923-933
    • (2008) EMBO J. , vol.27 , pp. 923-933
    • Burkhardt, P.1    Hattendorf, D.A.2    Weis, W.I.3    Fasshauer, D.4
  • 6
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman E.R. How does synaptotagmin trigger neurotransmitter release?. Annu. Rev. Biochem. 77 (2008) 615-641
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 7
    • 0036017804 scopus 로고    scopus 로고
    • SNAP-25 and synaptotagmin 1 function in Ca2+-dependent reversible docking of granules to the plasma membrane
    • Chieregatti E., Witkin J.W., and Baldini G. SNAP-25 and synaptotagmin 1 function in Ca2+-dependent reversible docking of granules to the plasma membrane. Traffic 3 (2002) 496-511
    • (2002) Traffic , vol.3 , pp. 496-511
    • Chieregatti, E.1    Witkin, J.W.2    Baldini, G.3
  • 8
    • 33847269603 scopus 로고    scopus 로고
    • 2+-phospholipid complex in neurotransmitter release
    • 2+-phospholipid complex in neurotransmitter release. J. Mol. Biol. 367 (2007) 848-863
    • (2007) J. Mol. Biol. , vol.367 , pp. 848-863
    • Dai, H.1    Shen, N.2    Arac, D.3    Rizo, J.4
  • 12
    • 1542320073 scopus 로고    scopus 로고
    • A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly
    • Fasshauer D., and Margittai M. A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly. J. Biol. Chem. 279 (2004) 7613-7621
    • (2004) J. Biol. Chem. , vol.279 , pp. 7613-7621
    • Fasshauer, D.1    Margittai, M.2
  • 13
  • 15
    • 33751290691 scopus 로고    scopus 로고
    • Rab27 and its effectors in secretory granule exocytosis: a novel docking machinery composed of a Rab27.effector complex
    • Fukuda M. Rab27 and its effectors in secretory granule exocytosis: a novel docking machinery composed of a Rab27.effector complex. Biochem. Soc. Trans. 34 (2006) 691-695
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 691-695
    • Fukuda, M.1
  • 22
    • 0028828226 scopus 로고
    • Defective recycling of synaptic vesicles in synaptotagmin mutants of C. elegans
    • Jorgensen E.M., Hartwieg E., Schuske K., Nonet M.L., Jin Y., and Horvitz H.R. Defective recycling of synaptic vesicles in synaptotagmin mutants of C. elegans. Nature 378 (1995) 196-198
    • (1995) Nature , vol.378 , pp. 196-198
    • Jorgensen, E.M.1    Hartwieg, E.2    Schuske, K.3    Nonet, M.L.4    Jin, Y.5    Horvitz, H.R.6
  • 23
    • 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., Dai H., Rizo J., and Südhof T.C. Dual modes of Munc18-1/SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminus. J. Neurosci. 27 (2007) 12147-12155
    • (2007) J. Neurosci. , vol.27 , pp. 12147-12155
    • Khvotchev, M.1    Dulubova, I.2    Sun, J.3    Dai, H.4    Rizo, J.5    Südhof, T.C.6
  • 26
    • 0037130255 scopus 로고    scopus 로고
    • The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo
    • Mackler J.M., Drummond J.A., Loewen C.A., Robinson I.M., and Reist N.E. The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo. Nature 418 (2002) 340-344
    • (2002) Nature , vol.418 , pp. 340-344
    • Mackler, J.M.1    Drummond, J.A.2    Loewen, C.A.3    Robinson, I.M.4    Reist, N.E.5
  • 27
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens S., Kozlov M.M., and McMahon H.T. How synaptotagmin promotes membrane fusion. Science 316 (2007) 1205-1208
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 28
    • 38349018454 scopus 로고    scopus 로고
    • Munc18-1 prevents the formation of ectopic SNARE complexes in living cells
    • Medine C.N., Rickman C., Chamberlain L.H., and Duncan R.R. Munc18-1 prevents the formation of ectopic SNARE complexes in living cells. J. Cell Sci. 120 (2007) 4407-4415
    • (2007) J. Cell Sci. , vol.120 , pp. 4407-4415
    • Medine, C.N.1    Rickman, C.2    Chamberlain, L.H.3    Duncan, R.R.4
  • 30
    • 0028104256 scopus 로고
    • Neurobiology: mice sans synaptotagmin
    • Neher E., and Penner R. Neurobiology: mice sans synaptotagmin. Nature 372 (1994) 316-317
    • (1994) Nature , vol.372 , pp. 316-317
    • Neher, E.1    Penner, R.2
  • 32
    • 33746915109 scopus 로고    scopus 로고
    • N- to C-terminal SNARE complex assembly promotes rapid membrane fusion
    • Pobbati A.V., Stein A., and Fasshauer D. N- to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 313 (2006) 673-676
    • (2006) Science , vol.313 , pp. 673-676
    • Pobbati, A.V.1    Stein, A.2    Fasshauer, D.3
  • 33
    • 0032188811 scopus 로고    scopus 로고
    • Morphologically docked synaptic vesicles are reduced in synaptotagmin mutants of Drosophila
    • Reist N.E., Buchanan J., Li J., DiAntonio A., Buxton E.M., and Schwarz T.L. Morphologically docked synaptic vesicles are reduced in synaptotagmin mutants of Drosophila. J. Neurosci. 18 (1998) 7662-7673
    • (1998) J. Neurosci. , vol.18 , pp. 7662-7673
    • Reist, N.E.1    Buchanan, J.2    Li, J.3    DiAntonio, A.4    Buxton, E.M.5    Schwarz, T.L.6
  • 34
    • 1842477457 scopus 로고    scopus 로고
    • Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate
    • Rickman C., Archer D.A., Meunier F.A., Craxton M., Fukuda M., Burgoyne R.D., and Davletov B. Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate. J. Biol. Chem. 279 (2004) 12574-12579
    • (2004) J. Biol. Chem. , vol.279 , pp. 12574-12579
    • Rickman, C.1    Archer, D.A.2    Meunier, F.A.3    Craxton, M.4    Fukuda, M.5    Burgoyne, R.D.6    Davletov, B.7
  • 37
    • 0032198135 scopus 로고    scopus 로고
    • A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex
    • Salem N., Faúndez V., Horng J.-T., and Kelly R.B. A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex. Nat. Neurosci. 1 (1998) 551-556
    • (1998) Nat. Neurosci. , vol.1 , pp. 551-556
    • Salem, N.1    Faúndez, V.2    Horng, J.-T.3    Kelly, R.B.4
  • 38
    • 0031019926 scopus 로고    scopus 로고
    • Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE SNAP-25, can explain docked vesicles at neurotoxin-treated synapses
    • Schiavo G., Stenbeck G., Rothman J.E., and Söllner T. Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Proc. Natl. Acad. Sci. USA 94 (1997) 997-1001
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.4
  • 40
    • 20444467326 scopus 로고    scopus 로고
    • A dual function for Munc-18 in exocytosis of PC12 cells
    • Schütz D., Zilly F., Lang T., Jahn R., and Bruns D. A dual function for Munc-18 in exocytosis of PC12 cells. Eur. J. Neurosci. 21 (2005) 2419-2432
    • (2005) Eur. J. Neurosci. , vol.21 , pp. 2419-2432
    • Schütz, D.1    Zilly, F.2    Lang, T.3    Jahn, R.4    Bruns, D.5
  • 41
    • 33845987734 scopus 로고    scopus 로고
    • Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
    • Shen J., Tareste D.C., Paumet F., Rothman J.E., and Melia T.J. Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. Cell 128 (2007) 183-195
    • (2007) Cell , vol.128 , pp. 183-195
    • Shen, J.1    Tareste, D.C.2    Paumet, F.3    Rothman, J.E.4    Melia, T.J.5
  • 43
    • 0038107577 scopus 로고    scopus 로고
    • Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23
    • Sørensen J.B., Nagy G., Varoqueaux F., Nehring R.B., Brose N., Wilson M.C., and Neher E. Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23. Cell 114 (2003) 75-86
    • (2003) Cell , vol.114 , pp. 75-86
    • Sørensen, J.B.1    Nagy, G.2    Varoqueaux, F.3    Nehring, R.B.4    Brose, N.5    Wilson, M.C.6    Neher, E.7
  • 45
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J., Maximov A., Shin O.H., Dai H., Rizo J., and Südhof T.C. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126 (2006) 1175-1187
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3    Dai, H.4    Rizo, J.5    Südhof, T.C.6
  • 46
    • 35748984692 scopus 로고    scopus 로고
    • Munc18-1 in secretion: lonely Munc joins SNARE team and takes control
    • Toonen R.F., and Verhage M. Munc18-1 in secretion: lonely Munc joins SNARE team and takes control. Trends Neurosci. 30 (2007) 564-572
    • (2007) Trends Neurosci. , vol.30 , pp. 564-572
    • Toonen, R.F.1    Verhage, M.2
  • 48
    • 49749084725 scopus 로고    scopus 로고
    • Vesicle docking in regulated exocytosis
    • Verhage M., and Sørensen J.B. Vesicle docking in regulated exocytosis. Traffic 9 (2008) 1414-1424
    • (2008) Traffic , vol.9 , pp. 1414-1424
    • Verhage, M.1    Sørensen, J.B.2
  • 50
    • 0035949679 scopus 로고    scopus 로고
    • Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I
    • Voets T., Moser T., Lund P.E., Chow R.H., Geppert M., Südhof T.C., and Neher E. Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I. Proc. Natl. Acad. Sci. USA 98 (2001) 11680-11685
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11680-11685
    • Voets, T.1    Moser, T.2    Lund, P.E.3    Chow, R.H.4    Geppert, M.5    Südhof, T.C.6    Neher, E.7
  • 52
    • 15544382560 scopus 로고    scopus 로고
    • Synaptic vesicle docking: a putative role for the Munc18/Sec1 protein family
    • Weimer R.M., and Richmond J.E. Synaptic vesicle docking: a putative role for the Munc18/Sec1 protein family. Curr. Top. Dev. Biol. 65 (2005) 83-113
    • (2005) Curr. Top. Dev. Biol. , vol.65 , pp. 83-113
    • Weimer, R.M.1    Richmond, J.E.2
  • 54
    • 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., Chu S., and Brünger A.T. Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16 (2008) 308-320
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brünger, A.T.5
  • 55
    • 0035066645 scopus 로고    scopus 로고
    • The neuronal t-SNARE complex is a parallel four-helix bundle
    • Xiao W., Poirier M.A., Bennett M.K., and Shin Y.K. The neuronal t-SNARE complex is a parallel four-helix bundle. Nat. Struct. Biol. 8 (2001) 308-311
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 308-311
    • Xiao, W.1    Poirier, M.A.2    Bennett, M.K.3    Shin, Y.K.4
  • 56
    • 55549100557 scopus 로고    scopus 로고
    • The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function
    • Xue M., Ma C., Craig T.K., Rosenmund C., and Rizo J. The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function. Nat. Struct. Mol. Biol. 15 (2008) 1160-1168
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1160-1168
    • Xue, M.1    Ma, C.2    Craig, T.K.3    Rosenmund, C.4    Rizo, J.5
  • 58
    • 33750241320 scopus 로고    scopus 로고
    • Munc18-Bound Syntaxin Readily Forms SNARE Complexes with Synaptobrevin in Native Plasma Membranes
    • Zilly F.E., Sørensen J.B., Jahn R., and Lang T. Munc18-Bound Syntaxin Readily Forms SNARE Complexes with Synaptobrevin in Native Plasma Membranes. PLoS Biol. 4 (2006) e330
    • (2006) PLoS Biol. , vol.4
    • Zilly, F.E.1    Sørensen, J.B.2    Jahn, R.3    Lang, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.