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Volumn 448, Issue 4, 2004, Pages 347-362

Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles

Author keywords

Calcium; Capacitance measurement; Chromaffin cell; Exocytosis; Membrane fusion; Neurosecretion; SNAP 25; SNARE; Synaptotagmin

Indexed keywords

PHOSPHOLIPID BINDING PROTEIN;

EID: 3442879896     PISSN: 00316768     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (136)

References (126)
  • 2
    • 0034710645 scopus 로고    scopus 로고
    • Intracellular calcium dependence of transmitter release rates at a fast central synapse
    • Schneggenburger R, Neher E (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
  • 3
    • 0034637149 scopus 로고    scopus 로고
    • Calcium sensitivity of glutamate release in a calyx-type terminal
    • Bollmann JH, Sakmann B, Borst JG (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
  • 4
    • 76549163887 scopus 로고
    • A quantitative study of end-plate potentials in isolated human muscle
    • Lond
    • Elmqvist D, Quastel DM (1965) A quantitative study of end-plate potentials in isolated human muscle. J Physiol (Lond) 178:505-529
    • (1965) J Physiol , vol.178 , pp. 505-529
    • Elmqvist, D.1    Quastel, D.M.2
  • 5
    • 0026709643 scopus 로고
    • Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components
    • Bittner MA, Holz RW (1992) Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components. J Biol Chem 267:16219-16225
    • (1992) J Biol Chem , vol.267 , pp. 16219-16225
    • Bittner, M.A.1    Holz, R.W.2
  • 6
    • 0027409301 scopus 로고
    • Multiple calcium-dependent processes related to secretion in bovine chromaffin cells
    • Neher E, Zucker RS (1993) Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron 10:21-30
    • (1993) Neuron , vol.10 , pp. 21-30
    • Neher, E.1    Zucker, R.S.2
  • 7
    • 0027772671 scopus 로고
    • A Ca-dependent early step in the release of catecholamines from adrenal chromaffin cells
    • Ruden L von, Neher E (1993) A Ca-dependent early step in the release of catecholamines from adrenal chromaffin cells. Science 262:1061-1065
    • (1993) Science , vol.262 , pp. 1061-1065
    • Von Ruden, L.1    Neher, E.2
  • 10
    • 0028862292 scopus 로고
    • Docked granules, the exocytic burst, and the need for ATP hydrolysis in endocrine cells
    • Parsons TD, Coorssen JR, Horstmarm H, Almers W (1995) Docked granules, the exocytic burst, and the need for ATP hydrolysis in endocrine cells. Neuron 15:1085-1096
    • (1995) Neuron , vol.15 , pp. 1085-1096
    • Parsons, T.D.1    Coorssen, J.R.2    Horstmarm, H.3    Almers, W.4
  • 11
    • 0030855088 scopus 로고    scopus 로고
    • Transport, docking and exocytosis of single secretory granules in live chromaffin cells
    • Steyer JA, Horstmann H, Almers W (1997) Transport, docking and exocytosis of single secretory granules in live chromaffin cells. Nature 388:474-478
    • (1997) Nature , vol.388 , pp. 474-478
    • Steyer, J.A.1    Horstmann, H.2    Almers, W.3
  • 12
    • 0036673069 scopus 로고    scopus 로고
    • Snares and Munc18 in synaptic vesicle fusion
    • Rizo J, Sudhof TC (2002) Snares and Munc18 in synaptic vesicle fusion. Nat Rev Neurosci 3:641-653
    • (2002) Nat Rev Neurosci , vol.3 , pp. 641-653
    • Rizo, J.1    Sudhof, T.C.2
  • 13
    • 0037672843 scopus 로고    scopus 로고
    • The molecular machinery of synaptic vesicle exocytosis
    • Li L, Chin LS (2003) The molecular machinery of synaptic vesicle exocytosis. Cell Mol Life Sci 60:942-960
    • (2003) Cell Mol Life Sci , vol.60 , pp. 942-960
    • Li, L.1    Chin, L.S.2
  • 14
    • 0037174660 scopus 로고    scopus 로고
    • ++-triggered exocytosis
    • ++-triggered exocytosis. Science 298:781-785
    • (2002) Science , vol.298 , pp. 781-785
    • Rettig, J.1    Neher, E.2
  • 15
    • 0036151862 scopus 로고    scopus 로고
    • Molecular determinants of exocytosis
    • Bruns D, Jahn R (2002) Molecular determinants of exocytosis. Pflugers Arch 443:333-338
    • (2002) Pflugers Arch , vol.443 , pp. 333-338
    • Bruns, D.1    Jahn, R.2
  • 16
    • 0037144587 scopus 로고    scopus 로고
    • Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell
    • Chen JL, Ahluwalia JP, Stamnes M (2002) Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell. J Biol Chem 277:35682-35687
    • (2002) J Biol Chem , vol.277 , pp. 35682-35687
    • Chen, J.L.1    Ahluwalia, J.P.2    Stamnes, M.3
  • 17
    • 0034814061 scopus 로고    scopus 로고
    • Secretion in alveolar type II cells at the interface of constitutive and regulated exocytosis
    • Frick M, Eschertzhuber S, Haller T, Mair N, Dietl P (2001) Secretion in alveolar type II cells at the interface of constitutive and regulated exocytosis. Am J Respir Cell Mol Biol 25:306-315
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 306-315
    • Frick, M.1    Eschertzhuber, S.2    Haller, T.3    Mair, N.4    Dietl, P.5
  • 19
    • 0029764204 scopus 로고    scopus 로고
    • 2+ triggers massive exocytosis in Chinese hamster ovary cells
    • 2+ triggers massive exocytosis in Chinese hamster ovary cells. EMBO J 15:3787-3791
    • (1996) EMBO J , vol.15 , pp. 3787-3791
    • Coorssen, J.R.1    Schmitt, H.2    Almers, W.3
  • 20
    • 0032008553 scopus 로고    scopus 로고
    • 2+ microdomains: New tools for understanding their roles in neurotransmitter release
    • 2+ microdomains: new tools for understanding their roles in neurotransmitter release. Neuron 20:389-399
    • (1998) Neuron , vol.20 , pp. 389-399
    • Neher, E.1
  • 21
    • 0027937697 scopus 로고
    • Releasable pools and the kinetics of exocytosis in adrenal chromaffin cells
    • Horrigan FT, Bookman RJ (1994) Releasable pools and the kinetics of exocytosis in adrenal chromaffin cells. Neuron 13:1119-1129
    • (1994) Neuron , vol.13 , pp. 1119-1129
    • Horrigan, F.T.1    Bookman, R.J.2
  • 22
    • 0033166461 scopus 로고    scopus 로고
    • Mechanisms underlying phasic and sustained secretion in chromaffin cells from mouse adrenal slices
    • Voets T, Neher E, Moser T (1999) Mechanisms underlying phasic and sustained secretion in chromaffin cells from mouse adrenal slices. Neuron 23:607-615
    • (1999) Neuron , vol.23 , pp. 607-615
    • Voets, T.1    Neher, E.2    Moser, T.3
  • 25
    • 0033622509 scopus 로고    scopus 로고
    • 2+-dependent steps leading to secretion in chromaffin cells from mouse adrenal slices
    • 2+-dependent steps leading to secretion in chromaffin cells from mouse adrenal slices. Neuron 28:537-545
    • (2000) Neuron , vol.28 , pp. 537-545
    • Voets, T.1
  • 26
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu T, Binz T, Niemann H, Neher E (1998) Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nat Neurosci 1:192-200
    • (1998) Nat Neurosci , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 27
    • 0033598965 scopus 로고    scopus 로고
    • Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis
    • Xu T, Rammner B, Margittai M, Artalejo AR, Neher E, Jahn R (1999) Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis. Cell 99:713-722
    • (1999) Cell , vol.99 , pp. 713-722
    • Xu, T.1    Rammner, B.2    Margittai, M.3    Artalejo, A.R.4    Neher, E.5    Jahn, R.6
  • 29
    • 0036310678 scopus 로고    scopus 로고
    • 2+ channels accounts for first-phase insulin secretion in mouse beta-cells
    • 2+ channels accounts for first-phase insulin secretion in mouse beta-cells. Diabetes 51 (Suppl 1):S74-S82
    • (2002) Diabetes , vol.51 , Issue.1 SUPPL.
    • Barg, S.1    Eliasson, L.2    Renstrom, E.3    Rorsman, P.4
  • 32
    • 0029782660 scopus 로고    scopus 로고
    • Simultaneous capacitance and amperometric measurements of exocytosis: A comparison
    • . 32. Oberhauser AF, Robinson IM, Fernandez JM (1996) Simultaneous capacitance and amperometric measurements of exocytosis: a comparison. Biophys J 71:1131-1139
    • (1996) Biophys J , vol.71 , pp. 1131-1139
    • Oberhauser, A.F.1    Robinson, I.M.2    Fernandez, J.M.3
  • 34
    • 0031919679 scopus 로고    scopus 로고
    • Comparison of secretory responses as measured by membrane capacitance and by amperometry
    • Haller M, Heinemann C, Chow RH, Heidelberger R, Neher E (1998) Comparison of secretory responses as measured by membrane capacitance and by amperometry. Biophys J 74:2100-2113
    • (1998) Biophys J , vol.74 , pp. 2100-2113
    • Haller, M.1    Heinemann, C.2    Chow, R.H.3    Heidelberger, R.4    Neher, E.5
  • 35
    • 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 PE, Chow RH, Geppert M, Sudhof TC, Neher E (2001) Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I. Proc Natl Acad Sci USA 98:11680-11685
    • (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    Sudhof, T.C.6    Neher, E.7
  • 36
    • 0030958610 scopus 로고    scopus 로고
    • 2+-activated exocytosis in a cell-free system
    • 2+-activated exocytosis in a cell-free system. J Biol Chem 272:14447-14453
    • (1997) J Biol Chem , vol.272 , pp. 14447-14453
    • Martin, T.F.1    Kowalchyk, J.A.2
  • 40
    • 0033068160 scopus 로고    scopus 로고
    • 2+-dependent exocytosis: Implications of kinetic diversity for secretory function
    • 2+-dependent exocytosis: implications of kinetic diversity for secretory function. Trends Neurosci 22:88-93
    • (1999) Trends Neurosci , vol.22 , pp. 88-93
    • Kasai, H.1
  • 41
    • 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
  • 42
    • 0043161982 scopus 로고    scopus 로고
    • Tuning exocytosis for speed: Fast and slow modes
    • Martin TF (2003) Tuning exocytosis for speed: fast and slow modes. Biochim Biophys Acta 1641:157-165
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 157-165
    • Martin, T.F.1
  • 43
    • 0024603065 scopus 로고
    • MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis
    • Holz RW, Bittner MA, Peppers SC, Senter RA, Eberhard DA (1989) MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis. J Biol Chem 264:5412-5419
    • (1989) J Biol Chem , vol.264 , pp. 5412-5419
    • Holz, R.W.1    Bittner, M.A.2    Peppers, S.C.3    Senter, R.A.4    Eberhard, D.A.5
  • 44
    • 0026664632 scopus 로고
    • Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins
    • Hay JC, Martin TF (1992) Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins. J Cell Biol 119:139-151
    • (1992) J Cell Biol , vol.119 , pp. 139-151
    • Hay, J.C.1    Martin, T.F.2
  • 45
    • 0033564814 scopus 로고    scopus 로고
    • Early requirement for alpha-SNAP and NSF in the secretory cascade in chromaffin cells
    • Xu T, Ashery U, Burgoyne RD, Neher E (1999) Early requirement for alpha-SNAP and NSF in the secretory cascade in chromaffin cells. EMBO J 18:3293-3304
    • (1999) EMBO J , vol.18 , pp. 3293-3304
    • Xu, T.1    Ashery, U.2    Burgoyne, R.D.3    Neher, E.4
  • 46
    • 0030176052 scopus 로고    scopus 로고
    • Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules
    • Gillis KD, Mossner R, Neher E (1996) Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules. Neuron 16:1209-1220
    • (1996) Neuron , vol.16 , pp. 1209-1220
    • Gillis, K.D.1    Mossner, R.2    Neher, E.3
  • 47
    • 0033556325 scopus 로고    scopus 로고
    • 2+activation of protein kinase C
    • 2+activation of protein kinase C. J Neurosci 19:589-598
    • (1999) J Neurosci , vol.19 , pp. 589-598
    • Smith, C.1
  • 48
    • 0032081255 scopus 로고    scopus 로고
    • 2+ acts by two separate pathways to modulate the supply of release-competent vesicles in chromaffin cells
    • 2+ acts by two separate pathways to modulate the supply of release-competent vesicles in chromaffin cells. Neuron 20:1243-1253
    • (1998) Neuron , vol.20 , pp. 1243-1253
    • Smith, C.1    Moser, T.2    Xu, T.3    Neher, E.4
  • 49
    • 0036848611 scopus 로고    scopus 로고
    • Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment
    • Nagy G, Matti U, Nehring RB, Binz T, Rettig J, Neher E, Sørensen JB (2002) Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment. J Neurosci 22:9278-9286
    • (2002) J Neurosci , vol.22 , pp. 9278-9286
    • Nagy, G.1    Matti, U.2    Nehring, R.B.3    Binz, T.4    Rettig, J.5    Neher, E.6    Sørensen, J.B.7
  • 50
    • 0023042529 scopus 로고
    • Guanine nucleotide effects on catecholamine secretion from digitonin-permeabilized adrenal chromaffin cells
    • Bittner MA, Holz RW, Neubig RR (1986) Guanine nucleotide effects on catecholamine secretion from digitonin-permeabilized adrenal chromaffin cells. J Biol Chem 261:10182-10188
    • (1986) J Biol Chem , vol.261 , pp. 10182-10188
    • Bittner, M.A.1    Holz, R.W.2    Neubig, R.R.3
  • 51
    • 0023107813 scopus 로고
    • Enhancement of stimulation-evoked catecholamine release from cultured bovine adrenal chromaffin cells by forskolin
    • Morita K, Dohi T, Kitayama S, Koyama Y, Tsujimoto A (1987) Enhancement of stimulation-evoked catecholamine release from cultured bovine adrenal chromaffin cells by forskolin. J Neurochem 48:243-247
    • (1987) J Neurochem , vol.48 , pp. 243-247
    • Morita, K.1    Dohi, T.2    Kitayama, S.3    Koyama, Y.4    Tsujimoto, A.5
  • 52
    • 0023664912 scopus 로고
    • Cyclic AMP inhibits both nicotine-induced actin disassembly and catecholamine secretion from bovine adrenal chromaffin cells
    • Cheek TR, Burgoyne RD (1987) Cyclic AMP inhibits both nicotine-induced actin disassembly and catecholamine secretion from bovine adrenal chromaffin cells. J Biol Chem 262:11663-11666
    • (1987) J Biol Chem , vol.262 , pp. 11663-11666
    • Cheek, T.R.1    Burgoyne, R.D.2
  • 53
    • 1242306711 scopus 로고    scopus 로고
    • Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25
    • Nagy G, Matti U, Binz T, Rettig J, Neher E, Sørensen JB (2004) Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25. Neuron 41:417-29
    • (2004) Neuron , vol.41 , pp. 417-429
    • Nagy, G.1    Matti, U.2    Binz, T.3    Rettig, J.4    Neher, E.5    Sørensen, J.B.6
  • 54
    • 0041659220 scopus 로고    scopus 로고
    • Structural insights into the SNARE mechanism
    • Fasshauer D (2003) Structural insights into the SNARE mechanism. Biochim Biophys Acta 1641:87-97
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 87-97
    • Fasshauer, D.1
  • 55
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395:347-353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 56
  • 58
    • 0029984090 scopus 로고    scopus 로고
    • 2+-induced and GTP analogue-induced catecholamine release from permeabilised adrenal chromaffin cells
    • 2+-induced and GTP analogue-induced catecholamine release from permeabilised adrenal chromaffin cells. FEBS Lett 386:137-140
    • (1996) FEBS Lett , vol.386 , pp. 137-140
    • Glenn, D.E.1    Burgoyne, R.D.2
  • 59
    • 0024313053 scopus 로고
    • Isolated light chain of tetanus toxin inhibits exocytosis: Studies in digitonin-permeabilized cells
    • Bittner MA, Habig WH, Holz RW (1989) Isolated light chain of tetanus toxin inhibits exocytosis: studies in digitonin-permeabilized cells. J Neurochem 53:966-968
    • (1989) J Neurochem , vol.53 , pp. 966-968
    • Bittner, M.A.1    Habig, W.H.2    Holz, R.W.3
  • 60
    • 0342751280 scopus 로고    scopus 로고
    • Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25
    • Wei S, Xu T, Ashery U, Kollewe A, Matti U, Antonin W, Rettig J, Neher E (2000) Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25. EMBO J 19:1279-1289
    • (2000) EMBO J , vol.19 , pp. 1279-1289
    • Wei, S.1    Xu, T.2    Ashery, U.3    Kollewe, A.4    Matti, U.5    Antonin, W.6    Rettig, J.7    Neher, E.8
  • 62
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner T, Bennett MK, Whiteheart SW, Scheller RH, Rothman JE (1993) A protein assembly-disassembly 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    Scheller, R.H.4    Rothman, J.E.5
  • 63
    • 0029835084 scopus 로고    scopus 로고
    • Patch-clamp capacitance analysis of the effects of alpha-SNAP on exocytosis in adrenal chromaffin cells
    • Kibble AV, Barnard RJ, Burgoyne RD (1996) Patch-clamp capacitance analysis of the effects of alpha-SNAP on exocytosis in adrenal chromaffin cells. J Cell Sci 109:2417-2422
    • (1996) J Cell Sci , vol.109 , pp. 2417-2422
    • Kibble, A.V.1    Barnard, R.J.2    Burgoyne, R.D.3
  • 65
    • 0037135984 scopus 로고    scopus 로고
    • SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs
    • Lang T, Margittai M, Holzler H, Jahn R (2002) SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs. J Cell Biol 158:751-760
    • (2002) J Cell Biol , vol.158 , pp. 751-760
    • Lang, T.1    Margittai, M.2    Holzler, H.3    Jahn, R.4
  • 69
    • 0032849774 scopus 로고    scopus 로고
    • An efficient method for infection of adrenal chromaffin cells using the Semliki Forest virus gene expression system
    • Ashery U, Betz A, Xu T, Brose N, Rettig J (1999) An efficient method for infection of adrenal chromaffin cells using the Semliki Forest virus gene expression system. Eur J Cell Biol 78:525-532
    • (1999) Eur J Cell Biol , vol.78 , pp. 525-532
    • Ashery, U.1    Betz, A.2    Xu, T.3    Brose, N.4    Rettig, J.5
  • 70
    • 0028968182 scopus 로고
    • Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development
    • Bark IC, Hahn KM, Ryabinin AE, Wilson MC (1995) Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development. Proc Natl Acad Sci USA 92:1510-1514
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1510-1514
    • Bark, I.C.1    Hahn, K.M.2    Ryabinin, A.E.3    Wilson, M.C.4
  • 71
    • 0029929223 scopus 로고    scopus 로고
    • Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues
    • Ravichandran V, Chawla A, Roche PA (1996) Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. J Biol Chem 271:13300-13303
    • (1996) J Biol Chem , vol.271 , pp. 13300-13303
    • Ravichandran, V.1    Chawla, A.2    Roche, P.A.3
  • 73
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann C, Sato K, Wickner W (1998) Defining the functions of trans-SNARE pairs. Nature 396:543-548
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 75
    • 0035034079 scopus 로고    scopus 로고
    • Sequential SNARE assembly underlies priming and triggering of exocytosis
    • Chen YA, Scales SJ, Scheller RH (2001) Sequential SNARE assembly underlies priming and triggering of exocytosis. Neuron 30:161-170
    • (2001) Neuron , vol.30 , pp. 161-170
    • Chen, Y.A.1    Scales, S.J.2    Scheller, R.H.3
  • 78
    • 0034082054 scopus 로고    scopus 로고
    • Regulation of transmitter release by Une-13 and its homologues
    • Brose N, Rosenmund C, Rettig J (2000) Regulation of transmitter release by Une-13 and its homologues. Curr Opin Neurobiol 10:303-311
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 303-311
    • Brose, N.1    Rosenmund, C.2    Rettig, J.3
  • 79
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin I, Rosenmund C, Sudhof TC, Brose N (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    Brose, N.4
  • 81
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond JE, Weimer RM, Jorgensen EM (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
  • 84
    • 0037377234 scopus 로고    scopus 로고
    • Vesicle trafficking: Pleasure and pain from SM genes
    • Toonen RF, Verhage M (2003) Vesicle trafficking: pleasure and pain from SM genes. Trends Cell Biol 13:177-186
    • (2003) Trends Cell Biol , vol.13 , pp. 177-186
    • Toonen, R.F.1    Verhage, M.2
  • 85
    • 0028102686 scopus 로고
    • rop, aDrosophila homolog of yeast Sec1 and vertebrate n-Sec1/Munc-18 proteins, is a negative regulator of neurotransmitter release in vivo
    • Schulze KL, Littleton JT, Salzberg A, Halachmi N, Stern M, Lev Z, Bellen HJ (1994) rop, aDrosophila homolog of yeast Sec1 and vertebrate n-Sec1/Munc-18 proteins, is a negative regulator of neurotransmitter release in vivo. Neuron 13:1099-1108
    • (1994) Neuron , vol.13 , pp. 1099-1108
    • Schulze, K.L.1    Littleton, J.T.2    Salzberg, A.3    Halachmi, N.4    Stern, M.5    Lev, Z.6    Bellen, H.J.7
  • 86
    • 0030719996 scopus 로고    scopus 로고
    • Evidence against an acute inhibitory role of nSec-1 (munc-18) in late steps of regulated exocytosis in chromaffin and PC12 cells
    • Graham ME, Sudlow AW, Burgoyne RD (1997) Evidence against an acute inhibitory role of nSec-1 (munc-18) in late steps of regulated exocytosis in chromaffin and PC12 cells. J Neurochem 69:2369-2377
    • (1997) J Neurochem , vol.69 , pp. 2369-2377
    • Graham, M.E.1    Sudlow, A.W.2    Burgoyne, R.D.3
  • 89
    • 0033198263 scopus 로고    scopus 로고
    • 2+-dependent activator protein for secretion is critical for the fusion of dense-core vesicles with the membrane in calf adrenal chromaffin cells
    • 2+-dependent activator protein for secretion is critical for the fusion of dense-core vesicles with the membrane in calf adrenal chromaffin cells. J Neurosci 19:7375-7383
    • (1999) J Neurosci , vol.19 , pp. 7375-7383
    • Elhamdani, A.1    Martin, T.F.2    Kowalchyk, J.A.3    Artalejo, C.R.4
  • 90
    • 0032478796 scopus 로고    scopus 로고
    • Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis
    • Loyet KM, Kowalchyk JA, Chaudhary A, Chen J, Prestwich GD, Martin TF (1998) Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis. J Biol Chem 273:8337-8343
    • (1998) J Biol Chem , vol.273 , pp. 8337-8343
    • Loyet, K.M.1    Kowalchyk, J.A.2    Chaudhary, A.3    Chen, J.4    Prestwich, G.D.5    Martin, T.F.6
  • 92
    • 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 RW, Hlubek MD, Sorensen SD, Fisher SK, Balla T, Ozaki S, Prestwich GD, Stuenkel EL, Bittner MA (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
  • 93
    • 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 DA, Cooper CL, Low MG, Holz RW (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
  • 96
    • 0025939932 scopus 로고
    • Regulation of the formation of inositol phosphates by calcium, guanine nucleotides and ATP in digitonin-permeabilized bovine adrenal chromaffin cells
    • Eberhard DA, Holz RW (1991) Regulation of the formation of inositol phosphates by calcium, guanine nucleotides and ATP in digitonin-permeabilized bovine adrenal chromaffin cells. Biochem J 279:447-453
    • (1991) Biochem J , vol.279 , pp. 447-453
    • Eberhard, D.A.1    Holz, R.W.2
  • 98
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • Schiavo G, Gu QM, Prestwich GD, Sollner TH, Rothman JE (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    Sollner, T.H.4    Rothman, J.E.5
  • 99
    • 0042672953 scopus 로고    scopus 로고
    • Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells
    • Tucker WC, Edwardson JM, Bai J, Kim HJ, Martin TF, Chapman ER (2003) Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells. J Cell Biol 162:199-209
    • (2003) J Cell Biol , vol.162 , pp. 199-209
    • Tucker, W.C.1    Edwardson, J.M.2    Bai, J.3    Kim, H.J.4    Martin, T.F.5    Chapman, E.R.6
  • 100
    • 0027338262 scopus 로고
    • 2+ receptor controls the final steps in peptide secretion from pituitary melanotrophs
    • 2+ receptor controls the final steps in peptide secretion from pituitary melanotrophs. Neuron 11:93-104
    • (1993) Neuron , vol.11 , pp. 93-104
    • Thomas, P.1    Wong, J.G.2    Lee, A.K.3    Almers, W.4
  • 101
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • Heidelberger R, Heinemann C, Neher E, Matthews G (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
  • 102
    • 0035047237 scopus 로고    scopus 로고
    • Calcium dependence of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse
    • Beutner D, Voets T, Neher E, Moser T (2001) Calcium dependence of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse. Neuron 29:681-690
    • (2001) Neuron , vol.29 , pp. 681-690
    • Beutner, D.1    Voets, T.2    Neher, E.3    Moser, T.4
  • 103
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • Sudhof TC (2002) Synaptotagmins: why so many? J Biol Chem 277:7629-7632
    • (2002) J Biol Chem , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 105
    • 0036304982 scopus 로고    scopus 로고
    • 2+ sensor that triggers exocytosis?
    • 2+ sensor that triggers exocytosis? Nat Rev Mol Cell Biol 3:498-508
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 498-508
    • Chapman, E.R.1
  • 106
    • 0141960930 scopus 로고    scopus 로고
    • 2+ sensor for neurotransmitter release
    • 2+ sensor for neurotransmitter release. Trends Neurosci 26:413-422
    • (2003) Trends Neurosci , vol.26 , pp. 413-422
    • Koh, T.W.1    Bellen, H.J.2
  • 108
    • 0027319325 scopus 로고
    • Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin
    • Nonet ML, Grundahl K, Meyer BJ, Rand JB (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    Rand, J.B.4
  • 112
    • 0344012489 scopus 로고    scopus 로고
    • Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a non-additive manner
    • Wang P, Wang CT, Bai J, Jackson MB, Chapman ER (2003) Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a non-additive manner. J Biol Chem 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
  • 113
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara M, Littleton JT (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
  • 115
    • 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    Sudhof, T.C.6
  • 117
    • 0041346213 scopus 로고    scopus 로고
    • The synaptotagmin C2A domain is part of the calcium sensor controlling fast synaptic transmission
    • Stevens CF, Sullivan JM (2003) The synaptotagmin C2A domain is part of the calcium sensor controlling fast synaptic transmission. Neuron 39:299-308
    • (2003) Neuron , vol.39 , pp. 299-308
    • Stevens, C.F.1    Sullivan, J.M.2
  • 119
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release - Four years of SNARE complexes
    • Hanson PI, Heuser JE, Jahn R (1997) Neurotransmitter release - four years of SNARE complexes. Curr Opin Neurobiol 7:310-315
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 120
    • 0027176212 scopus 로고
    • A two-step model of secretion control in neuroendocrine cells
    • Heinemann C, von Ruden L, Chow RH, Neher E (1993) A two-step model of secretion control in neuroendocrine cells. Pflugers Arch 424:105-112
    • (1993) Pflugers Arch , vol.424 , pp. 105-112
    • Heinemann, C.1    Von Ruden, L.2    Chow, R.H.3    Neher, E.4
  • 121
    • 0028978947 scopus 로고
    • Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis
    • Chamberlain LH, Roth D, Morgan A, Burgoyne RD (1995) Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis. J Cell Biol 130:1063-1070
    • (1995) J Cell Biol , vol.130 , pp. 1063-1070
    • Chamberlain, L.H.1    Roth, D.2    Morgan, A.3    Burgoyne, R.D.4
  • 122
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale ML, Seward EP, Trifaro JM (1995) Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14:353-363
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaro, J.M.3
  • 123
    • 0035071322 scopus 로고    scopus 로고
    • Phosphorylation of snapin by PKA modulates its interaction with the SNARE complex
    • Chheda MG, Ashery U, Thakur P, Rettig J, Sheng ZH (2001) Phosphorylation of snapin by PKA modulates its interaction with the SNARE complex. Nat Cell Biol 3:331-338
    • (2001) Nat Cell Biol , vol.3 , pp. 331-338
    • Chheda, M.G.1    Ashery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.H.5
  • 124
    • 0026742966 scopus 로고
    • A temperature-sensitive step in exocytosis
    • Bittner MA, Holz RW (1992) A temperature-sensitive step in exocytosis. J Biol Chem 267:16226-16229
    • (1992) J Biol Chem , vol.267 , pp. 16226-16229
    • Bittner, M.A.1    Holz, R.W.2
  • 125
    • 0034668835 scopus 로고    scopus 로고
    • The readily releasable pool of vesicles in chromaffin cells is replenished in a temperature-dependent manner and transiently overfills at 37°C
    • Dinkelacker V, Voets T, Neher E, Moser T (2000) The readily releasable pool of vesicles in chromaffin cells is replenished in a temperature-dependent manner and transiently overfills at 37°C. J Neurosci 20:8377-8383
    • (2000) J Neurosci , vol.20 , pp. 8377-8383
    • Dinkelacker, V.1    Voets, T.2    Neher, E.3    Moser, T.4
  • 126
    • 0034908225 scopus 로고    scopus 로고
    • SV2 modulates the size of the readily releasable pool of secretory vesicles
    • Xu T, Bajjalieh SM (2001) SV2 modulates the size of the readily releasable pool of secretory vesicles. Nat Cell Biol 3:691-698
    • (2001) Nat Cell Biol , vol.3 , pp. 691-698
    • Xu, T.1    Bajjalieh, S.M.2


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