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Volumn 162, Issue 2, 2003, Pages 199-209

Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells

Author keywords

C2 domain; Exocytosis; Membrane fusion; SNARE; Synaptotagmin

Indexed keywords

CALCIUM; CATECHOLAMINE; ISOPROTEIN; MEMBRANE PROTEIN; PEPTIDE FRAGMENT; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNAPTOTAGMIN I; SYNAPTOTAGMIN IX; SYNTAXIN; UNCLASSIFIED DRUG;

EID: 0042672953     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200302060     Document Type: Article
Times cited : (98)

References (66)
  • 1
    • 0035368680 scopus 로고    scopus 로고
    • How does calcium trigger neurotransmitter release?
    • Augustine, G.J. 2001. How does calcium trigger neurotransmitter release? Curr. Opin. Neurobiol. 11:320-326.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 320-326
    • Augustine, G.J.1
  • 2
    • 0037274615 scopus 로고    scopus 로고
    • 2+-triggered synaptotagmin C2 domain-membrane interactions
    • 2+-triggered synaptotagmin C2 domain-membrane interactions. Methods Enzymol. 360:238-258.
    • (2003) Methods Enzymol. , vol.360 , pp. 238-258
    • Bai, J.1    Chapman, E.R.2
  • 3
    • 0037022307 scopus 로고    scopus 로고
    • 2+-triggered membrane penetration activity within the C2B domain of synaptotagmin I
    • 2+-triggered membrane penetration activity within the C2B domain of synaptotagmin I. Proc. Natl. Acad. Sci. USA. 99:1665-1670.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1665-1670
    • Bai, J.1    Wang, P.2    Chapman, E.R.3
  • 4
    • 0034637149 scopus 로고    scopus 로고
    • Calcium sensitivity of glutamate release in a calyx-type terminal
    • Bollmann, J.H., B. Sakmann, and J.G. Borst. 2000. Calcium sensitivity of glutamate release in a calyx-type terminal. Science. 289:953-957.
    • (2000) Science , vol.289 , pp. 953-957
    • Bollmann, J.H.1    Sakmann, B.2    Borst, J.G.3
  • 5
    • 0027269605 scopus 로고
    • Inhibition of neurotransmittet release by C2-domain peptides implicates synaptotagmin in exocytosis
    • Bommert, K., M.P. Charlton, W.M. DeBello, G.J. Chin, H. Betz, and G.J. Augustine. 1993. Inhibition of neurotransmittet release by C2-domain peptides implicates synaptotagmin in exocytosis. Nature. 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
    • 0015517310 scopus 로고
    • The lipid composition of adult rat brain synaptosomal plasma membranes
    • Breckenridge, W.C., G. Gombos, and I.G. Morgan. 1972. The lipid composition of adult rat brain synaptosomal plasma membranes. Biochim. Biophys. Acta. 266:695-707.
    • (1972) Biochim. Biophys. Acta , vol.266 , pp. 695-707
    • Breckenridge, W.C.1    Gombos, G.2    Morgan, I.G.3
  • 7
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose, N., A.G. Petrenko, T.C. Siidhof, and R. Jahn. 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    Siidhof, T.C.3    Jahn, R.4
  • 8
    • 0028068586 scopus 로고
    • 2+-dependent interaction of the cytoplasmic region of synaptotagmin with membranes: Autonomous function of a single C2-homologous domain
    • 2+-dependent interaction of the cytoplasmic region of synaptotagmin with membranes: autonomous function of a single C2-homologous domain. J. Biol. Chem. 269:5735-5741.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5735-5741
    • Chapman, E.R.1    Jahn, R.2
  • 9
  • 12
    • 0035417439 scopus 로고    scopus 로고
    • Genomic analysis of synaptotagmin genes
    • Craxton, M. 2001. Genomic analysis of synaptotagmin genes. Genomics. 77:43-49.
    • (2001) Genomics , vol.77 , pp. 43-49
    • Craxton, M.1
  • 13
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse
    • Cremona, O., and P. De Camilli. 2001. Phosphoinositides in membrane traffic at the synapse. J. Cell Sci. 114:1041-1052.
    • (2001) J. Cell Sci. , vol.114 , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 16
    • 0028351171 scopus 로고
    • The effect on synaptic physiology of synaptotagmin mutations in Drosophila
    • DiAntonio, A., and T.L. Schwarz. 1994. The effect on synaptic physiology of synaptotagmin mutations in Drosophila. Neuron. 12:909-920.
    • (1994) Neuron , vol.12 , pp. 909-920
    • DiAntonio, A.1    Schwarz, T.L.2
  • 17
    • 0035904238 scopus 로고    scopus 로고
    • 2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis
    • 2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis. J. Cell Biol. 154:1117-1123.
    • (2001) J. Cell Biol. , vol.154 , pp. 1117-1123
    • Earles, C.A.1    Bai, J.2    Wang, P.3    Chapman, E.R.4
  • 18
    • 0025330471 scopus 로고
    • Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP
    • Eberhard, D.A., C.L. Cooper, M.G. Low, and R.W. Holz. 1990. Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP. Biochem. J. 268:15-25.
    • (1990) Biochem. J , vol.268 , pp. 15-25
    • Eberhard, D.A.1    Cooper, C.L.2    Low, M.G.3    Holz, R.W.4
  • 19
    • 0027459033 scopus 로고
    • A role for synaptotagmin (p65) in regulated exocytosis
    • Elferink, L.A., M.R. Peterson, and R.H. Scheller. 1993. A role for synaptotagmin (p65) in regulated exocytosis. Cell. 72:153-159.
    • (1993) Cell , vol.72 , pp. 153-159
    • Elferink, L.A.1    Peterson, M.R.2    Scheller, R.H.3
  • 22
    • 0034623083 scopus 로고    scopus 로고
    • Distinct self-oligomerization activities of synaptotagmin family. Unique calcium-dependent oligomerization properties of synaptotagmin VII
    • Fukuda, M., and K. Mikoshiba. 2000. Distinct self-oligomerization activities of synaptotagmin family. Unique calcium-dependent oligomerization properties of synaptotagmin VII. J. Biol. Chem. 275:28180-28185.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28180-28185
    • Fukuda, M.1    Mikoshiba, K.2
  • 23
    • 0035920141 scopus 로고    scopus 로고
    • Mechanism of the calcium-dependent multimerization of synaptotagmin VII mediated by its first and second C2 domains
    • Fukuda, M., and K. Mikoshiba. 2001. Mechanism of the calcium-dependent multimerization of synaptotagmin VII mediated by its first and second C2 domains. J. Biol. Chem. 276:27670-27676.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27670-27676
    • Fukuda, M.1    Mikoshiba, K.2
  • 24
    • 0033615704 scopus 로고    scopus 로고
    • Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X
    • Fukuda, M., E. Kanno, and K. Mikoshiba. 1999. Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X. J. Biol. Chem. 274:31421-31427.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31421-31427
    • Fukuda, M.1    Kanno, E.2    Mikoshiba, K.3
  • 26
    • 0036645672 scopus 로고    scopus 로고
    • Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and human
    • Fukuda, M., Y. Ogata, C. Saegusa, E. Kanno, and K. Mikoshiba. 2002b. Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and human. Biochem. J. 365:173-180.
    • (2002) Biochem. J , vol.365 , pp. 173-180
    • Fukuda, M.1    Ogata, Y.2    Saegusa, C.3    Kanno, E.4    Mikoshiba, K.5
  • 27
    • 0037474271 scopus 로고    scopus 로고
    • Nerve growth factor-dependent sorting of synaptotagmin IV protein to mature dense-core vesicles that undergo calcium-dependent exocytosis in PC12 cells
    • Fukuda, M., E. Kanno, Y. Ogata, C. Saegusa, T. Kim, Y.P. Loh, and A. Yamamoto. 2003. Nerve growth factor-dependent sorting of synaptotagmin IV protein to mature dense-core vesicles that undergo calcium-dependent exocytosis in PC12 cells. J. Biol. Chem. 278:3220-3226.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3220-3226
    • Fukuda, M.1    Kanno, E.2    Ogata, Y.3    Saegusa, C.4    Kim, T.5    Loh, Y.P.6    Yamamoto, A.7
  • 30
  • 32
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • Heidelberger, R., C. Heinemann, E. Neher, and G. Matthews. 1994. Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature. 371:513-515.
    • (1994) Nature , vol.371 , pp. 513-515
    • Heidelberger, R.1    Heinemann, C.2    Neher, E.3    Matthews, G.4
  • 33
    • 0034625410 scopus 로고    scopus 로고
    • A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis
    • Holz, R.W., M.D. Hlubek, S.D. Sorensen, S.K. Fisher, T. Balla, S. Ozaki, G.D. Prestwich, E.L. Stuenkel, and M.A. Bittner. 2000. A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis. J. Biol. Chem. 275:17878-17885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17878-17885
    • Holz, R.W.1    Hlubek, M.D.2    Sorensen, S.D.3    Fisher, S.K.4    Balla, T.5    Ozaki, S.6    Prestwich, G.D.7    Stuenkel, E.L.8    Bittner, M.A.9
  • 34
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R., and T.C. Siidhof. 1999. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68:863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Siidhof, T.C.2
  • 35
    • 0028828226 scopus 로고
    • Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans
    • Jorgensen, E.M., E. Hartwieg, K. Schuske, M.L. Nonet, Y. Jin, and H.R. Horvitz. 1995. Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans. Nature. 378:196-199.
    • (1995) Nature , vol.378 , pp. 196-199
    • Jorgensen, E.M.1    Hartwieg, E.2    Schuske, K.3    Nonet, M.L.4    Jin, Y.5    Horvitz, H.R.6
  • 36
    • 0031727008 scopus 로고    scopus 로고
    • Large dense-core vesicle exocytosis in PC12 cells
    • Klenchin, V.A., J.A. Kowalchyk, and T.F. Martin. 1998. Large dense-core vesicle exocytosis in PC12 cells. Methods. 16:204-208.
    • (1998) Methods , vol.16 , pp. 204-208
    • Klenchin, V.A.1    Kowalchyk, J.A.2    Martin, T.F.3
  • 38
    • 0027974130 scopus 로고
    • 2+ dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • 2+ dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc. Natl. Acad Sci. USA. 91:10888-10892.
    • (1994) Proc. Natl. Acad Sci. USA , vol.91 , pp. 10888-10892
    • Littleton, J.T.1    Stern, M.2    Perin, M.3    Bellen, H.J.4
  • 39
    • 0033584339 scopus 로고    scopus 로고
    • Synaptic function modulated by changes in the ratio of synaptotagmin I and IV
    • Littleton, J.T., T.L. Serano, G.M. Rubin, B. Ganetzky, and E.R. Chapman. 1999. Synaptic function modulated by changes in the ratio of synaptotagmin I and IV. Nature. 400:757-760.
    • (1999) Nature , vol.400 , pp. 757-760
    • Littleton, J.T.1    Serano, T.L.2    Rubin, G.M.3    Ganetzky, B.4    Chapman, E.R.5
  • 42
    • 0019851385 scopus 로고
    • Identification of a synaptic vesicle-specific protein with a wide tissue distribution in neuronal and neurosecretory tissue
    • Matthew, W.D., L. Tsavaler, and L.F. Reichardt. 1981. Identification of a synaptic vesicle-specific protein with a wide tissue distribution in neuronal and neurosecretory tissue. J. Cell Biol. 91:257-269.
    • (1981) J. Cell Biol. , vol.91 , pp. 257-269
    • Matthew, W.D.1    Tsavaler, L.2    Reichardt, L.F.3
  • 43
    • 0028305903 scopus 로고
    • Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells
    • Mizuta, M., N. Inagaki, Y. Nemoto, S. Matsukura, M. Takahashi, and S. Seino. 1994. Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells. J. Biol. Chem. 269:11675-11678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11675-11678
    • Mizuta, M.1    Inagaki, N.2    Nemoto, Y.3    Matsukura, S.4    Takahashi, M.5    Seino, S.6
  • 44
    • 0033607279 scopus 로고    scopus 로고
    • Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain
    • Parlati, F., T. Weber, J.A. McNew, B. Westermann, T.H. Söllner, and J.E. Rothman. 1999. Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain. Proc. Natl. Acad. Sci. USA. 96:12565-12570.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12565-12570
    • Parlati, F.1    Weber, T.2    McNew, J.A.3    Westermann, B.4    Söllner, T.H.5    Rothman, J.E.6
  • 45
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin, M.S., V.A. Fried, G.A. Mignery, R. Jahn, and T.C. Siidhof. 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    Jahn, R.4    Siidhof, T.C.5
  • 48
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • Schiavo, G., Q.M. Gu, G.D. Prestwich, T.H. Söllner, and J.E. Rothman. 1996. Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin. Proc. Natl. Acad. Sci. USA. 93:13327-13332.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13327-13332
    • Schiavo, G.1    Gu, Q.M.2    Prestwich, G.D.3    Söllner, T.H.4    Rothman, J.E.5
  • 49
    • 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., G. Stenbeck, J.E. Rothman, and T.H. Söllner. 1997. 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. 94:997-1001.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 50
    • 0034710645 scopus 로고    scopus 로고
    • Intracellular calcium dependence of transmitter release rates at a fast central synapse
    • Schneggenburger, R., and E. Neher. 2000. Intracellular calcium dependence of transmitter release rates at a fast central synapse. Nature. 406:889-893.
    • (2000) Nature , vol.406 , pp. 889-893
    • Schneggenburger, R.1    Neher, E.2
  • 51
    • 0036307988 scopus 로고    scopus 로고
    • Synaptotagmin function in dense core vesicle exocytosis studied in cracked PC12 cells
    • Shin, O.H., J. Rizo, and T.C. Südhof. 2002. Synaptotagmin function in dense core vesicle exocytosis studied in cracked PC12 cells. Nat. Neurosci. 5:649-656.
    • (2002) Nat. Neurosci. , vol.5 , pp. 649-656
    • Shin, O.H.1    Rizo, J.2    Südhof, T.C.3
  • 52
    • 0037427025 scopus 로고    scopus 로고
    • 2+ binding site of the synaptotagmin 1 C2B domain triggers fast exocytosis without stimulating SNARE interactions
    • 2+ binding site of the synaptotagmin 1 C2B domain triggers fast exocytosis without stimulating SNARE interactions. Neuron. 37:99-108.
    • (2003) Neuron , vol.37 , pp. 99-108
    • Shin, O.H.1    Rhee, J.S.2    Tang, J.3    Sugita, S.4    Rosenmund, C.5    Südhof, T.C.6
  • 60
    • 0028901750 scopus 로고
    • Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain
    • Vician, L., I.K. Lim, G. Ferguson, G. Tocco, M. Baudry, and H.R. Herschman. 1995. Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain. Proc. Natl. Acad. Sci. USA. 92:2164-2168.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2164-2168
    • Vician, L.1    Lim, I.K.2    Ferguson, G.3    Tocco, G.4    Baudry, M.5    Herschman, H.R.6
  • 61
    • 0035798162 scopus 로고    scopus 로고
    • Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles
    • Wang, C.T., R. Grishanin, C.A. Earles, P.Y. Chang, T.F. Martin, E.R. Chapman, and M.B. Jackson. 2001. Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles. Science. 294:1111-1115.
    • (2001) Science , vol.294 , pp. 1111-1115
    • Wang, C.T.1    Grishanin, R.2    Earles, C.A.3    Chang, P.Y.4    Martin, T.F.5    Chapman, E.R.6    Jackson, M.B.7
  • 63
    • 0023076597 scopus 로고
    • Lipid composition and orientation in secretory vesicles
    • Westhead, E.W. 1987. Lipid composition and orientation in secretory vesicles. Ann. NY Acad. Sci. 493:92-100.
    • (1987) Ann. NY Acad. Sci. , vol.493 , pp. 92-100
    • Westhead, E.W.1
  • 65
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara, M., and J.T. Littleton. 2002. Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release. Neuron. 36:897-908.
    • (2002) Neuron , vol.36 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2


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