메뉴 건너뛰기




Volumn 49, Issue 1, 2012, Pages 1-8

Ca 2+-independent syntaxin binding to the C 2B effector region of synaptotagmin

Author keywords

Exocytosis; Neurotransmitter release; SNAP 25; Synaptic vesicle; Synaptobrevin

Indexed keywords

CALCIUM ION; COMPLEMENT COMPONENT C2B; EGTAZIC ACID; SNARE PROTEIN; SODIUM CHLORIDE; SYNAPTOBREVIN 2; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNAPTOTAGMIN I; SYNTAXIN; SYNTAXIN 1;

EID: 82355187664     PISSN: 10447431     EISSN: 10959327     Source Type: Journal    
DOI: 10.1016/j.mcn.2011.09.007     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 0035368680 scopus 로고    scopus 로고
    • How does calcium trigger neurotransmitter release?
    • Augustine G.J. How does calcium trigger neurotransmitter release?. Curr. Opin. Neurobiol. 2001, 11:320-326.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 320-326
    • Augustine, G.J.1
  • 2
    • 0842291506 scopus 로고    scopus 로고
    • 2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • 2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat. Struct. Mol. Biol. 2004, 11:36-44.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 3
    • 1842475284 scopus 로고    scopus 로고
    • Fusion pore dynamics are regulated by synaptotagmin.t-SNARE interactions
    • Bai J., Wang C.T., Richards D.A., Jackson M.B., Chapman E.R. Fusion pore dynamics are regulated by synaptotagmin.t-SNARE interactions. Neuron 2004, 41:929-942.
    • (2004) Neuron , vol.41 , pp. 929-942
    • Bai, J.1    Wang, C.T.2    Richards, D.A.3    Jackson, M.B.4    Chapman, E.R.5
  • 4
    • 0026778460 scopus 로고
    • Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett M.K., Calakos N., Scheller R.H. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 1992, 257:255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 5
    • 0027269605 scopus 로고
    • Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis
    • Bommert K., Charlton M.P., DeBello W.M., Chin G.J., Betz H., Augustine G.J. Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis. Nature 1993, 363:163-165.
    • (1993) Nature , vol.363 , pp. 163-165
    • Bommert, K.1    Charlton, M.P.2    DeBello, W.M.3    Chin, G.J.4    Betz, H.5    Augustine, G.J.6
  • 6
    • 20444370233 scopus 로고    scopus 로고
    • Synaptotagmin mutants Y311N and K326/327A alter the calcium dependence of neurotransmission
    • Borden C.R., Stevens C.F., Sullivan J.M., Zhu Y. Synaptotagmin mutants Y311N and K326/327A alter the calcium dependence of neurotransmission. Mol. Cell. Neurosci. 2005, 29:462-470.
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 462-470
    • Borden, C.R.1    Stevens, C.F.2    Sullivan, J.M.3    Zhu, Y.4
  • 7
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman E.R. How does synaptotagmin trigger neurotransmitter release?. Annu. Rev. Biochem. 2008, 77:615-641.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 9
    • 33847269603 scopus 로고    scopus 로고
    • 2+-phospholipid complex in neurotransmitter release
    • 2+-phospholipid complex in neurotransmitter release. J. Mol. Biol. 2007, 367:848-863.
    • (2007) J. Mol. Biol. , vol.367 , pp. 848-863
    • Dai, H.1    Shen, N.2    Araç, D.3    Rizo, J.4
  • 14
    • 33747453911 scopus 로고    scopus 로고
    • Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains
    • Herrick D.Z., Sterbling S., Rasch K.A., Hinderliter A., Cafiso D.S. Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains. Biochemistry 2006, 45:9668-9674.
    • (2006) Biochemistry , vol.45 , pp. 9668-9674
    • Herrick, D.Z.1    Sterbling, S.2    Rasch, K.A.3    Hinderliter, A.4    Cafiso, D.S.5
  • 17
    • 0029917101 scopus 로고    scopus 로고
    • Localization of synaptotagmin-binding domains on syntaxin
    • Kee Y., Scheller R.H. Localization of synaptotagmin-binding domains on syntaxin. J. Neurosci. 1996, 16:1975-1981.
    • (1996) J. Neurosci. , vol.16 , pp. 1975-1981
    • Kee, Y.1    Scheller, R.H.2
  • 20
    • 0033975848 scopus 로고    scopus 로고
    • Calcium-dependent dissociation of synaptotagmin from synaptic SNARE complexes
    • Leveque C., Boudier J.A., Takahashi M., Seagar M. Calcium-dependent dissociation of synaptotagmin from synaptic SNARE complexes. J. Neurochem. 2000, 74:367-374.
    • (2000) J. Neurochem. , vol.74 , pp. 367-374
    • Leveque, C.1    Boudier, J.A.2    Takahashi, M.3    Seagar, M.4
  • 26
    • 0035898066 scopus 로고    scopus 로고
    • 2 domain of synaptotagmin disrupt synaptic transmission at Drosophila neuromuscular junctions
    • 2 domain of synaptotagmin disrupt synaptic transmission at Drosophila neuromuscular junctions. J. Comp. Neurol. 2001, 436:4-16.
    • (2001) J. Comp. Neurol. , vol.436 , pp. 4-16
    • Mackler, J.M.1    Reist, N.E.2
  • 27
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens S., Kozlov M.M., McMahon H.T. How synaptotagmin promotes membrane fusion. Science 2007, 316:1205-1208.
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 29
  • 30
    • 3042796387 scopus 로고    scopus 로고
    • Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons
    • Nishiki T., Augustine G.J. Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons. J. Neurosci. 2004, 24:6127-6132.
    • (2004) J. Neurosci. , vol.24 , pp. 6127-6132
    • Nishiki, T.1    Augustine, G.J.2
  • 31
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Nishiki T., Kamata Y., Nemoto Y., Omori A., Ito T., Takahashi M., Kozaki S. Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J. Biol. Chem. 1994, 269:10498-10503.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6    Kozaki, S.7
  • 32
    • 0028966170 scopus 로고
    • Expression and complex formation of soluble N-ethyl-maleimide-sensitive factor attachment protein (SNAP) receptors in clonal rat endocrine cells
    • Oho C., Seino S., Takahashi M. Expression and complex formation of soluble N-ethyl-maleimide-sensitive factor attachment protein (SNAP) receptors in clonal rat endocrine cells. Neurosci. Lett. 1995, 186:208-210.
    • (1995) Neurosci. Lett. , vol.186 , pp. 208-210
    • Oho, C.1    Seino, S.2    Takahashi, M.3
  • 33
    • 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., 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. 2004, 279:12574-12579.
    • (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
  • 34
    • 0037458711 scopus 로고    scopus 로고
    • Mechanism of calcium-independent synaptotagmin binding to target SNAREs
    • Rickman C., Davletov B. Mechanism of calcium-independent synaptotagmin binding to target SNAREs. J. Biol. Chem. 2003, 278:5501-5504.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5501-5504
    • Rickman, C.1    Davletov, B.2
  • 36
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature 1994, 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 37
    • 0028922592 scopus 로고
    • Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins
    • Schiavo G., Shone C.C., Bennett M.K., Scheller R.H., Montecucco C. Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins. J. Biol. Chem. 1995, 270:10566-10570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10566-10570
    • Schiavo, G.1    Shone, C.C.2    Bennett, M.K.3    Scheller, R.H.4    Montecucco, C.5
  • 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., Söllner T.H. 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. U. S. A. 1997, 94:997-1001.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 40
    • 0029898850 scopus 로고    scopus 로고
    • Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release
    • Shimazaki Y., Nishiki T., Omori A., Sekiguchi M., Kamata Y., Kozaki S., Takahashi M. Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release. J. Biol. Chem. 1996, 271:14548-14553.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14548-14553
    • Shimazaki, Y.1    Nishiki, T.2    Omori, A.3    Sekiguchi, M.4    Kamata, Y.5    Kozaki, S.6    Takahashi, M.7
  • 43
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner T., Bennett M.K., Whiteheart S.W., Scheller R.H., Rothman J.E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 1993, 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
  • 45
  • 47
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution
    • Sutton R.B., Fasshauer D., Jahn R., Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution. Nature 1998, 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 49
    • 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., Südhof T.C. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 2006, 126:1175-1187.
    • (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
  • 50
    • 0344012489 scopus 로고    scopus 로고
    • Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner
    • Wang P., Wang C.T., Bai J., Jackson M.B., Chapman E.R. Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner. J. Biol. Chem. 2003, 278:47030-47037.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47030-47037
    • Wang, P.1    Wang, C.T.2    Bai, J.3    Jackson, M.B.4    Chapman, E.R.5
  • 52
    • 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., Brunger A.T. Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 2008, 16:308-320.
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 53
    • 0010983324 scopus 로고
    • The isolation and characterization of acetylcholine-containing particles from brain
    • Whittaker V.P. The isolation and characterization of acetylcholine-containing particles from brain. Biochem. J. 1959, 72:694-706.
    • (1959) Biochem. J. , vol.72 , pp. 694-706
    • Whittaker, V.P.1
  • 54
    • 0000040564 scopus 로고    scopus 로고
    • Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo
    • Wu M.N., Fergestad T., Lloyd T.E., He Y., Broadie K., Bellen H.J. Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo. Neuron 1999, 23:593-605.
    • (1999) Neuron , vol.23 , pp. 593-605
    • Wu, M.N.1    Fergestad, T.2    Lloyd, T.E.3    He, Y.4    Broadie, K.5    Bellen, H.J.6
  • 55
  • 56
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara M., Littleton J.T. Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release. Neuron 2002, 36:897-908.
    • (2002) Neuron , vol.36 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.