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Volumn 105, Issue 11, 2013, Pages 2507-2516

Conformational dynamics of calcium-triggered activation of fusion by synaptotagmin

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; SNAP25 PROTEIN, MOUSE; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN I; SYT1 PROTEIN, MOUSE;

EID: 84889579613     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.10.029     Document Type: Article
Times cited : (32)

References (59)
  • 1
    • 0000268186 scopus 로고
    • Electron microscope observations of interneuronal and neuromuscular synapses
    • G.E. Palade, and S.L. Palay Electron microscope observations of interneuronal and neuromuscular synapses Anat. Rec. 118 1954 335 336
    • (1954) Anat. Rec. , vol.118 , pp. 335-336
    • Palade, G.E.1    Palay, S.L.2
  • 3
    • 0002275807 scopus 로고
    • Submicroscopic vesicular component in the synapse
    • E.D.P. DeRobertis, and H.S. Bennett Submicroscopic vesicular component in the synapse Fed. Proc. 13 1954 35
    • (1954) Fed. Proc. , vol.13 , pp. 35
    • Derobertis, E.D.P.1    Bennett, H.S.2
  • 4
    • 76949136401 scopus 로고
    • Spontaneous subthreshold activity at motor nerve endings
    • P. Fatt, and B. Katz Spontaneous subthreshold activity at motor nerve endings J. Physiol. 117 1952 109 128
    • (1952) J. Physiol. , vol.117 , pp. 109-128
    • Fatt, P.1    Katz, B.2
  • 5
    • 0000194649 scopus 로고
    • The effect of calcium on acetylcholine release from motor nerve terminals
    • B. Katz, and R. Miledi The effect of calcium on acetylcholine release from motor nerve terminals Proc. R. Soc. Lond. B Biol. Sci. 161 1965 496 503
    • (1965) Proc. R. Soc. Lond. B Biol. Sci. , vol.161 , pp. 496-503
    • Katz, B.1    Miledi, R.2
  • 6
    • 0014078590 scopus 로고
    • The timing of calcium action during neuromuscular transmission
    • B. Katz, and R. Miledi The timing of calcium action during neuromuscular transmission J. Physiol. 189 1967 535 544
    • (1967) J. Physiol. , vol.189 , pp. 535-544
    • Katz, B.1    Miledi, R.2
  • 7
    • 0037841760 scopus 로고    scopus 로고
    • Fusion of cells by flipped SNAREs
    • C. Hu, and M. Ahmed J.E. Rothman Fusion of cells by flipped SNAREs Science 300 2003 1745 1749
    • (2003) Science , vol.300 , pp. 1745-1749
    • Hu, C.1    Ahmed, M.2    Rothman, J.E.3
  • 8
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • T. Söllner, and S.W. Whiteheart J.E. Rothman SNAP receptors implicated in vesicle targeting and fusion Nature 362 1993 318 324
    • (1993) Nature , vol.362 , pp. 318-324
    • Söllner, T.1    Whiteheart, S.W.2    Rothman, J.E.3
  • 9
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • T. Weber, and B.V. Zemelman J.E. Rothman SNAREpins: minimal machinery for membrane fusion Cell 92 1998 759 772
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    Rothman, J.E.3
  • 10
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • C.G. Giraudo, and W.S. Eng J.E. Rothman A clamping mechanism involved in SNARE-dependent exocytosis Science 313 2006 676 680
    • (2006) Science , vol.313 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Rothman, J.E.3
  • 11
    • 79961030875 scopus 로고    scopus 로고
    • Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state
    • F. Li, and F. Pincet J.E. Rothman Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state Nat. Struct. Mol. Biol. 18 2011 941 946
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 941-946
    • Li, F.1    Pincet, F.2    Rothman, J.E.3
  • 13
    • 0035282457 scopus 로고    scopus 로고
    • Synaptotagmin i functions as a calcium regulator of release probability
    • R. Fernández-Chacón, and A. Königstorfer T.C. Südhof Synaptotagmin I functions as a calcium regulator of release probability Nature 410 2001 41 49
    • (2001) Nature , vol.410 , pp. 41-49
    • Fernández-Chacón, R.1    Königstorfer, A.2    Südhof, T.C.3
  • 14
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • N. Brose, and A.G. Petrenko R. Jahn Synaptotagmin: a calcium sensor on the synaptic vesicle surface Science 256 1992 1021 1025
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Jahn, R.3
  • 15
    • 0028061861 scopus 로고
    • Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse
    • M. Geppert, and Y. Goda T.C. Südhof Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse Cell 79 1994 717 727
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Südhof, T.C.3
  • 16
    • 0027974130 scopus 로고
    • Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • J.T. Littleton, and M. Stern H.J. Bellen Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants Proc. Natl. Acad. Sci. USA 91 1994 10888 10892
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10888-10892
    • Littleton, J.T.1    Stern, M.2    Bellen, H.J.3
  • 17
    • 33845234610 scopus 로고    scopus 로고
    • A gain-of-function mutation in synaptotagmin-1 reveals a critical role of Ca2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis
    • Z.P. Pang, and O.H. Shin T.C. Südhof A gain-of-function mutation in synaptotagmin-1 reveals a critical role of Ca2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis J. Neurosci. 26 2006 12556 12565
    • (2006) J. Neurosci. , vol.26 , pp. 12556-12565
    • Pang, Z.P.1    Shin, O.H.2    Südhof, T.C.3
  • 18
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • M.S. Perin, and V.A. Fried T.C. Südhof Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C Nature 345 1990 260 263
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Südhof, T.C.3
  • 19
    • 58849105859 scopus 로고    scopus 로고
    • Alternative zippering as an on-off switch for SNARE-mediated fusion
    • C.G. Giraudo, and A. Garcia-Diaz J.E. Rothman Alternative zippering as an on-off switch for SNARE-mediated fusion Science 323 2009 512 516
    • (2009) Science , vol.323 , pp. 512-516
    • Giraudo, C.G.1    Garcia-Diaz, A.2    Rothman, J.E.3
  • 20
    • 84864878312 scopus 로고    scopus 로고
    • Complexin arrests a pool of docked vesicles for fast Ca2+-dependent release
    • J. Malsam, and D. Parisotto T.H. Söllner Complexin arrests a pool of docked vesicles for fast Ca2+-dependent release EMBO J. 31 2012 3270 3281
    • (2012) EMBO J. , vol.31 , pp. 3270-3281
    • Malsam, J.1    Parisotto, D.2    Söllner, T.H.3
  • 21
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • T.C. Südhof, and J.E. Rothman Membrane fusion: grappling with SNARE and SM proteins Science 323 2009 474 477
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 22
    • 0028859443 scopus 로고
    • Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain
    • M. Fukuda, and T. Kojima K. Mikoshiba Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain J. Biol. Chem. 270 1995 26523 26527
    • (1995) J. Biol. Chem. , vol.270 , pp. 26523-26527
    • Fukuda, M.1    Kojima, T.2    Mikoshiba, K.3
  • 23
    • 0034682759 scopus 로고    scopus 로고
    • Membrane-embedded synaptotagmin penetrates cis or trans target membranes and clusters via a novel mechanism
    • J. Bai, and C.A. Earles E.R. Chapman Membrane-embedded synaptotagmin penetrates cis or trans target membranes and clusters via a novel mechanism J. Biol. Chem. 275 2000 25427 25435
    • (2000) J. Biol. Chem. , vol.275 , pp. 25427-25435
    • Bai, J.1    Earles, C.A.2    Chapman, E.R.3
  • 24
    • 0032577067 scopus 로고    scopus 로고
    • Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers
    • E.R. Chapman, and A.F. Davis Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers J. Biol. Chem. 273 1998 13995 14001
    • (1998) J. Biol. Chem. , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 25
    • 0033213302 scopus 로고    scopus 로고
    • Kinetics of synaptotagmin responses to Ca2+ and assembly with the core SNARE complex onto membranes
    • A.F. Davis, and J. Bai E.R. Chapman Kinetics of synaptotagmin responses to Ca2+ and assembly with the core SNARE complex onto membranes Neuron 24 1999 363 376
    • (1999) Neuron , vol.24 , pp. 363-376
    • Davis, A.F.1    Bai, J.2    Chapman, E.R.3
  • 26
    • 34948827535 scopus 로고    scopus 로고
    • Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids
    • A. Stein, and A. Radhakrishnan R. Jahn Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids Nat. Struct. Mol. Biol. 14 2007 904 911
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 904-911
    • Stein, A.1    Radhakrishnan, A.2    Jahn, R.3
  • 27
    • 33748442138 scopus 로고    scopus 로고
    • Ca2+-triggered simultaneous membrane penetration of the tandem C2-domains of synaptotagmin i
    • E. Hui, J. Bai, and E.R. Chapman Ca2+-triggered simultaneous membrane penetration of the tandem C2-domains of synaptotagmin I Biophys. J. 91 2006 1767 1777
    • (2006) Biophys. J. , vol.91 , pp. 1767-1777
    • Hui, E.1    Bai, J.2    Chapman, E.R.3
  • 28
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • J. Bai, W.C. Tucker, and E.R. Chapman PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane Nat. Struct. Mol. Biol. 11 2004 36 44
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 29
    • 1942520207 scopus 로고    scopus 로고
    • Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs
    • W.C. Tucker, T. Weber, and E.R. Chapman Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs Science 304 2004 435 438
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 30
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • S. Martens, M.M. Kozlov, and H.T. McMahon 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
  • 31
    • 50549084252 scopus 로고    scopus 로고
    • Ca2+-dependent, phospholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo
    • B.E. Paddock, and A.R. Striegel N.E. Reist Ca2+-dependent, phospholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo J. Neurosci. 28 2008 7458 7466
    • (2008) J. Neurosci. , vol.28 , pp. 7458-7466
    • Paddock, B.E.1    Striegel, A.R.2    Reist, N.E.3
  • 32
    • 79951529500 scopus 로고    scopus 로고
    • Membrane penetration by synaptotagmin is required for coupling calcium binding to vesicle fusion in vivo
    • B.E. Paddock, and Z. Wang N.E. Reist Membrane penetration by synaptotagmin is required for coupling calcium binding to vesicle fusion in vivo J. Neurosci. 31 2011 2248 2257
    • (2011) J. Neurosci. , vol.31 , pp. 2248-2257
    • Paddock, B.E.1    Wang, Z.2    Reist, N.E.3
  • 33
    • 29444436513 scopus 로고    scopus 로고
    • Augmenting neurotransmitter release by enhancing the apparent Ca2+ affinity of synaptotagmin 1
    • J.S. Rhee, and L.Y. Li C. Rosenmund Augmenting neurotransmitter release by enhancing the apparent Ca2+ affinity of synaptotagmin 1 Proc. Natl. Acad. Sci. USA 102 2005 18664 18669
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18664-18669
    • Rhee, J.S.1    Li, L.Y.2    Rosenmund, C.3
  • 34
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • L.V. Chernomordik, and M.M. Kozlov Protein-lipid interplay in fusion and fission of biological membranes Annu. Rev. Biochem. 72 2003 175 207
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 35
    • 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
    • S.S. Rathore, and E.G. Bend J. Shen 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 2010 22399 22406
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22399-22406
    • Rathore, S.S.1    Bend, E.G.2    Shen, J.3
  • 36
    • 79961028121 scopus 로고    scopus 로고
    • A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion
    • S.S. Krishnakumar, and D.T. Radoff J.E. Rothman A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion Nat. Struct. Mol. Biol. 18 2011 934 940
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 934-940
    • Krishnakumar, S.S.1    Radoff, D.T.2    Rothman, J.E.3
  • 37
    • 0037157825 scopus 로고    scopus 로고
    • Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin i
    • L.K. Mahal, and S.M. Sequeira T.H. Söllner Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I J. Cell Biol. 158 2002 273 282
    • (2002) J. Cell Biol. , vol.158 , pp. 273-282
    • Mahal, L.K.1    Sequeira, S.M.2    Söllner, T.H.3
  • 38
    • 84863338243 scopus 로고    scopus 로고
    • SNARE proteins: One to fuse and three to keep the nascent fusion pore open
    • L. Shi, and Q.T. Shen F. Pincet SNARE proteins: one to fuse and three to keep the nascent fusion pore open Science 335 2012 1355 1359
    • (2012) Science , vol.335 , pp. 1355-1359
    • Shi, L.1    Shen, Q.T.2    Pincet, F.3
  • 40
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • M. van de Weert, and L. Stella Fluorescence quenching and ligand binding: A critical discussion of a popular methodology J. Mol. Struct. 998 2011 144 150
    • (2011) J. Mol. Struct. , vol.998 , pp. 144-150
    • Van De Weert, M.1    Stella, L.2
  • 41
    • 71549142855 scopus 로고    scopus 로고
    • Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscs
    • T.K. Ritchie, and Y.V. Grinkova S.G. Sligar Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscs Methods Enzymol. 464 2009 211 231
    • (2009) Methods Enzymol. , vol.464 , pp. 211-231
    • Ritchie, T.K.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 42
    • 77949264921 scopus 로고    scopus 로고
    • Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex
    • U.B. Choi, and P. Strop K.R. Weninger Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex Nat. Struct. Mol. Biol. 17 2010 318 324
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 318-324
    • Choi, U.B.1    Strop, P.2    Weninger, K.R.3
  • 43
    • 0037204076 scopus 로고    scopus 로고
    • Three-dimensional structure of the complexin/SNARE complex
    • X. Chen, and D.R. Tomchick J. Rizo Three-dimensional structure of the complexin/SNARE complex Neuron 33 2002 397 409
    • (2002) Neuron , vol.33 , pp. 397-409
    • Chen, X.1    Tomchick, D.R.2    Rizo, J.3
  • 44
    • 0027960576 scopus 로고
    • Synergistic membrane interactions of the two C2 domains of synaptotagmin
    • C.K. Damer, and C.E. Creutz Synergistic membrane interactions of the two C2 domains of synaptotagmin J. Biol. Chem. 269 1994 31115 31123
    • (1994) J. Biol. Chem. , vol.269 , pp. 31115-31123
    • Damer, C.K.1    Creutz, C.E.2
  • 45
    • 33644804207 scopus 로고    scopus 로고
    • Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids
    • D. Araç, and X. Chen J. Rizo Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids Nat. Struct. Mol. Biol. 13 2006 209 217
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 209-217
    • Araç, D.1    Chen, X.2    Rizo, J.3
  • 46
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • G. Schiavo, and Q.M. Gu J.E. Rothman Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin Proc. Natl. Acad. Sci. USA 93 1996 13327 13332
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13327-13332
    • Schiavo, G.1    Gu, Q.M.2    Rothman, J.E.3
  • 47
    • 79960053907 scopus 로고    scopus 로고
    • Mechanism and function of synaptotagmin-mediated membrane apposition
    • E. Hui, and J.D. Gaffaney E.R. Chapman Mechanism and function of synaptotagmin-mediated membrane apposition Nat. Struct. Mol. Biol. 18 2011 813 821
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 813-821
    • Hui, E.1    Gaffaney, J.D.2    Chapman, E.R.3
  • 48
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • S. Takamori, and M. Holt R. Jahn Molecular anatomy of a trafficking organelle Cell 127 2006 831 846
    • (2006) Cell , vol.127 , pp. 831-846
    • Takamori, S.1    Holt, M.2    Jahn, R.3
  • 49
    • 0014601923 scopus 로고
    • Lipid composition of synaptic plasma membranes isolated from rat brain by zonal centrifugation
    • C. Cotman, and M.L. Blank F. Snyder Lipid composition of synaptic plasma membranes isolated from rat brain by zonal centrifugation Biochemistry 8 1969 4606 4612
    • (1969) Biochemistry , vol.8 , pp. 4606-4612
    • Cotman, C.1    Blank, M.L.2    Snyder, F.3
  • 50
    • 81855221892 scopus 로고    scopus 로고
    • Membrane protein sequestering by ionic protein-lipid interactions
    • G. van den Bogaart, and K. Meyenberg R. Jahn Membrane protein sequestering by ionic protein-lipid interactions Nature 479 2011 552 555
    • (2011) Nature , vol.479 , pp. 552-555
    • Van Den Bogaart, G.1    Meyenberg, K.2    Jahn, R.3
  • 51
    • 0028970788 scopus 로고
    • Ca2+ regulates the interaction between synaptotagmin and syntaxin 1
    • E.R. Chapman, and P.I. Hanson R. Jahn Ca2+ regulates the interaction between synaptotagmin and syntaxin 1 J. Biol. Chem. 270 1995 23667 23671
    • (1995) J. Biol. Chem. , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    Jahn, R.3
  • 52
    • 23144455040 scopus 로고    scopus 로고
    • Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex
    • M.E. Bowen, and K. Weninger A.T. Brunger Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex Biophys. J. 89 2005 690 702
    • (2005) Biophys. J. , vol.89 , pp. 690-702
    • Bowen, M.E.1    Weninger, K.2    Brunger, A.T.3
  • 53
    • 77949264920 scopus 로고    scopus 로고
    • Molecular mechanism of the synaptotagmin-SNARE interaction in Ca2+-triggered vesicle fusion
    • M. Vrljic, and P. Strop A.T. Brunger Molecular mechanism of the synaptotagmin-SNARE interaction in Ca2+-triggered vesicle fusion Nat. Struct. Mol. Biol. 17 2010 325 331
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 325-331
    • Vrljic, M.1    Strop, P.2    Brunger, A.T.3
  • 54
    • 70350025513 scopus 로고    scopus 로고
    • The Ca2+ affinity of synaptotagmin 1 is markedly increased by a specific interaction of its C2B domain with phosphatidylinositol 4,5-bisphosphate
    • A. Radhakrishnan, and A. Stein D. Fasshauer The Ca2+ affinity of synaptotagmin 1 is markedly increased by a specific interaction of its C2B domain with phosphatidylinositol 4,5-bisphosphate J. Biol. Chem. 284 2009 25749 25760
    • (2009) J. Biol. Chem. , vol.284 , pp. 25749-25760
    • Radhakrishnan, A.1    Stein, A.2    Fasshauer, D.3
  • 55
    • 84860871594 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate increases Ca2+ affinity of synaptotagmin-1 by 40-fold
    • G. van den Bogaart, and K. Meyenberg R. Jahn Phosphatidylinositol 4,5-bisphosphate increases Ca2+ affinity of synaptotagmin-1 by 40-fold J. Biol. Chem. 287 2012 16447 16453
    • (2012) J. Biol. Chem. , vol.287 , pp. 16447-16453
    • Van Den Bogaart, G.1    Meyenberg, K.2    Jahn, R.3
  • 56
    • 84870992389 scopus 로고    scopus 로고
    • Complexin controls spontaneous and evoked neurotransmitter release by regulating the timing and properties of synaptotagmin activity
    • R.A. Jorquera, and S. Huntwork-Rodriguez J.T. Littleton Complexin controls spontaneous and evoked neurotransmitter release by regulating the timing and properties of synaptotagmin activity J. Neurosci. 32 2012 18234 18245
    • (2012) J. Neurosci. , vol.32 , pp. 18234-18245
    • Jorquera, R.A.1    Huntwork-Rodriguez, S.2    Littleton, J.T.3
  • 57
    • 84877821540 scopus 로고    scopus 로고
    • Complexin facilitates exocytosis and synchronizes vesicle release in two secretory model systems
    • M.Y. Lin, and J.G. Rohan R.H. Chow Complexin facilitates exocytosis and synchronizes vesicle release in two secretory model systems J. Physiol. 591 2013 2463 2473
    • (2013) J. Physiol. , vol.591 , pp. 2463-2473
    • Lin, M.Y.1    Rohan, J.G.2    Chow, R.H.3
  • 58
    • 84881514823 scopus 로고    scopus 로고
    • Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion
    • J. Diao, and P. Grob A.T. Brunger Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion Elife 1 2012 e00109
    • (2012) Elife , vol.1 , pp. 00109
    • Diao, J.1    Grob, P.2    Brunger, A.T.3
  • 59
    • 67349106087 scopus 로고    scopus 로고
    • Synaptotagmin-1 functions as a Ca2+ sensor for spontaneous release
    • J. Xu, and Z.P. Pang T.C. Südhof Synaptotagmin-1 functions as a Ca2+ sensor for spontaneous release Nat. Neurosci. 12 2009 759 766
    • (2009) Nat. Neurosci. , vol.12 , pp. 759-766
    • Xu, J.1    Pang, Z.P.2    Südhof, T.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.