메뉴 건너뛰기




Volumn 9, Issue 12, 2013, Pages

A Sequential Vesicle Pool Model with a Single Release Sensor and a Ca2+-Dependent Priming Catalyst Effectively Explains Ca2+-Dependent Properties of Neurosecretion

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; LAKES; MAMMALS;

EID: 84892688353     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003362     Document Type: Article
Times cited : (30)

References (57)
  • 1
    • 76949136401 scopus 로고
    • Spontaneous subthreshold activity at motor nerve endings
    • Fatt P, Katz B, (1952) Spontaneous subthreshold activity at motor nerve endings. J Physiol 117: 109-128.
    • (1952) J Physiol , vol.117 , pp. 109-128
    • Fatt, P.1    Katz, B.2
  • 2
    • 0014075881 scopus 로고
    • On the relationship between calcium concentration and the amplitude of the end-plate potential
    • Dodge FA Jr, Rahamimoff R, (1967) On the relationship between calcium concentration and the amplitude of the end-plate potential. J Physiol 189: 90P-92P.
    • (1967) J Physiol , vol.189
    • Dodge Jr., F.A.1    Rahamimoff, R.2
  • 3
    • 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
  • 4
    • 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
  • 5
    • 19444365446 scopus 로고    scopus 로고
    • Allosteric modulation of the presynaptic Ca2+ sensor for vesicle fusion
    • Lou X, Scheuss V, Schneggenburger R, (2005) Allosteric modulation of the presynaptic Ca2+ sensor for vesicle fusion. Nature 435: 497-501.
    • (2005) Nature , vol.435 , pp. 497-501
    • Lou, X.1    Scheuss, V.2    Schneggenburger, R.3
  • 6
    • 0028000081 scopus 로고
    • Kinetics of the secretory response in bovine chromaffin cells following flash photolysis of caged Ca2+
    • Heinemann C, Chow RH, Neher E, Zucker RS, (1994) Kinetics of the secretory response in bovine chromaffin cells following flash photolysis of caged Ca2+. Biophys J 67: 2546-2557.
    • (1994) Biophys J , vol.67 , pp. 2546-2557
    • Heinemann, C.1    Chow, R.H.2    Neher, E.3    Zucker, R.S.4
  • 7
    • 0032529332 scopus 로고    scopus 로고
    • Calcium dependence and recovery kinetics of presynaptic depression at the climbing fiber to Purkinje cell synapse
    • Dittman JS, Regehr WG, (1998) Calcium dependence and recovery kinetics of presynaptic depression at the climbing fiber to Purkinje cell synapse. J Neurosci 18: 6147-6162.
    • (1998) J Neurosci , vol.18 , pp. 6147-6162
    • Dittman, J.S.1    Regehr, W.G.2
  • 8
    • 37549037512 scopus 로고    scopus 로고
    • Quantitative analysis of calcium-dependent vesicle recruitment and its functional role at the calyx of Held synapse
    • Hosoi N, Sakaba T, Neher E, (2007) Quantitative analysis of calcium-dependent vesicle recruitment and its functional role at the calyx of Held synapse. J Neurosci 27: 14286-14298.
    • (2007) J Neurosci , vol.27 , pp. 14286-14298
    • Hosoi, N.1    Sakaba, T.2    Neher, E.3
  • 9
    • 0027772671 scopus 로고
    • A Ca-dependent early step in the release of catecholamines from adrenal chromaffin cells
    • von Ruden L, 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
    • 52049106127 scopus 로고    scopus 로고
    • Multiple roles of calcium ions in the regulation of neurotransmitter release
    • Neher E, Sakaba T, (2008) Multiple roles of calcium ions in the regulation of neurotransmitter release. Neuron 59: 861-872.
    • (2008) Neuron , vol.59 , pp. 861-872
    • Neher, E.1    Sakaba, T.2
  • 11
    • 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
  • 12
    • 0032707610 scopus 로고    scopus 로고
    • Properties of a model of Ca++-dependent vesicle pool dynamics and short term synaptic depression
    • Weis S, Schneggenburger R, Neher E, (1999) Properties of a model of Ca++-dependent vesicle pool dynamics and short term synaptic depression. Biophys J 77: 2418-2429.
    • (1999) Biophys J , vol.77 , pp. 2418-2429
    • Weis, S.1    Schneggenburger, R.2    Neher, E.3
  • 13
    • 0037340258 scopus 로고    scopus 로고
    • Heterogeneous presynaptic release probabilities: functional relevance for short-term plasticity
    • Trommershauser J, Schneggenburger R, Zippelius A, Neher E, (2003) Heterogeneous presynaptic release probabilities: functional relevance for short-term plasticity. Biophys J 84: 1563-1579.
    • (2003) Biophys J , vol.84 , pp. 1563-1579
    • Trommershauser, J.1    Schneggenburger, R.2    Zippelius, A.3    Neher, E.4
  • 14
    • 65649117725 scopus 로고    scopus 로고
    • A general model of synaptic transmission and short-term plasticity
    • Pan B, Zucker RS, (2009) A general model of synaptic transmission and short-term plasticity. Neuron 62: 539-554.
    • (2009) Neuron , vol.62 , pp. 539-554
    • Pan, B.1    Zucker, R.S.2
  • 16
    • 0033622509 scopus 로고    scopus 로고
    • Dissection of three Ca2+-dependent steps leading to secretion in chromaffin cells from mouse adrenal slices
    • Voets T, (2000) Dissection of three Ca2+-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
  • 18
    • 0028061861 scopus 로고
    • Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse
    • Geppert M, Goda Y, Hammer RE, Li C, Rosahl TW, et al. (1994) Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse. Cell 79: 717-727.
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Hammer, R.E.3    Li, C.4    Rosahl, T.W.5
  • 19
    • 36749078085 scopus 로고    scopus 로고
    • A dual-Ca2+-sensor model for neurotransmitter release in a central synapse
    • Sun J, Pang ZP, Qin D, Fahim AT, Adachi R, et al. (2007) A dual-Ca2+-sensor model for neurotransmitter release in a central synapse. Nature 450: 676-682.
    • (2007) Nature , vol.450 , pp. 676-682
    • Sun, J.1    Pang, Z.P.2    Qin, D.3    Fahim, A.T.4    Adachi, R.5
  • 21
    • 34248584691 scopus 로고    scopus 로고
    • Synaptotagmin-1, -2, and -9: Ca(2+) sensors for fast release that specify distinct presynaptic properties in subsets of neurons
    • Xu J, Mashimo T, Sudhof TC, (2007) Synaptotagmin-1,-2, and-9: Ca(2+) sensors for fast release that specify distinct presynaptic properties in subsets of neurons. Neuron 54: 567-581.
    • (2007) Neuron , vol.54 , pp. 567-581
    • Xu, J.1    Mashimo, T.2    Sudhof, T.C.3
  • 22
    • 84872802734 scopus 로고    scopus 로고
    • Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release
    • Ma C, Su L, Seven AB, Xu Y, Rizo J, (2013) Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release. Science 339: 421-425.
    • (2013) Science , vol.339 , pp. 421-425
    • Ma, C.1    Su, L.2    Seven, A.B.3    Xu, Y.4    Rizo, J.5
  • 23
    • 77949266565 scopus 로고    scopus 로고
    • Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis
    • Shin OH, Lu J, Rhee JS, Tomchick DR, Pang ZP, et al. (2010) Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis. Nat Struct Mol Biol 17: 280-288.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 280-288
    • Shin, O.H.1    Lu, J.2    Rhee, J.S.3    Tomchick, D.R.4    Pang, Z.P.5
  • 24
    • 85027945821 scopus 로고    scopus 로고
    • Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex
    • Ma C, Li W, Xu Y, Rizo J, (2011) Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex. Nature structural & molecular biology 18: 542-549.
    • (2011) Nature Structural & Molecular Biology , vol.18 , pp. 542-549
    • Ma, C.1    Li, W.2    Xu, Y.3    Rizo, J.4
  • 25
    • 76349098018 scopus 로고    scopus 로고
    • Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis
    • Walter AM, Wiederhold K, Bruns D, Fasshauer D, Sorensen JB, (2010) Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis. J Cell Biol 188: 401-413.
    • (2010) J Cell Biol , vol.188 , pp. 401-413
    • Walter, A.M.1    Wiederhold, K.2    Bruns, D.3    Fasshauer, D.4    Sorensen, J.B.5
  • 26
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • Giraudo CG, Eng WS, Melia TJ, Rothman JE, (2006) A clamping mechanism involved in SNARE-dependent exocytosis. Science 313: 676-680.
    • (2006) Science , vol.313 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Melia, T.J.3    Rothman, J.E.4
  • 27
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J, Maximov A, Shin OH, Dai H, Rizo J, et al. (2006) A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 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
  • 28
    • 49449095255 scopus 로고    scopus 로고
    • Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+
    • Chicka MC, Hui E, Liu H, Chapman ER, (2008) Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+. Nat Struct Mol Biol 15: 827-835.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 827-835
    • Chicka, M.C.1    Hui, E.2    Liu, H.3    Chapman, E.R.4
  • 29
    • 78649930845 scopus 로고    scopus 로고
    • Complexin clamps asynchronous release by blocking a secondary Ca(2+) sensor via its accessory alpha helix
    • Yang X, Kaeser-Woo YJ, Pang ZP, Xu W, Sudhof TC, (2010) Complexin clamps asynchronous release by blocking a secondary Ca(2+) sensor via its accessory alpha helix. Neuron 68: 907-920.
    • (2010) Neuron , vol.68 , pp. 907-920
    • Yang, X.1    Kaeser-Woo, Y.J.2    Pang, Z.P.3    Xu, W.4    Sudhof, T.C.5
  • 30
    • 79951717108 scopus 로고    scopus 로고
    • Synaptotagmin increases the dynamic range of synapses by driving ca(2+)-evoked release and by clamping a near-linear remaining ca(2+) sensor
    • Kochubey O, Schneggenburger R, (2011) Synaptotagmin increases the dynamic range of synapses by driving ca(2+)-evoked release and by clamping a near-linear remaining ca(2+) sensor. Neuron 69: 736-748.
    • (2011) Neuron , vol.69 , pp. 736-748
    • Kochubey, O.1    Schneggenburger, R.2
  • 31
    • 32544460031 scopus 로고    scopus 로고
    • Different effects on fast exocytosis induced by synaptotagmin 1 and 2 isoforms and abundance but not by phosphorylation
    • Nagy G, Kim JH, Pang ZP, Matti U, Rettig J, et al. (2006) Different effects on fast exocytosis induced by synaptotagmin 1 and 2 isoforms and abundance but not by phosphorylation. J Neurosci 26: 632-643.
    • (2006) J Neurosci , vol.26 , pp. 632-643
    • Nagy, G.1    Kim, J.H.2    Pang, Z.P.3    Matti, U.4    Rettig, J.5
  • 32
    • 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
  • 33
    • 3442879896 scopus 로고    scopus 로고
    • Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles
    • Sorensen JB, (2004) Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles. Pflugers Archiv: European journal of physiology 448: 347-362.
    • (2004) Pflugers Archiv: European Journal of Physiology , vol.448 , pp. 347-362
    • Sorensen, J.B.1
  • 34
    • 84885441178 scopus 로고    scopus 로고
    • Doc2b Synchronizes Secretion from Chromaffin Cells by stimulating fast and Inhibiting Sustained Release
    • Pinheiro PS, De Wit H, Walter AM, Groffen AJ, Verhage M, et al. (2013) Doc2b Synchronizes Secretion from Chromaffin Cells by stimulating fast and Inhibiting Sustained Release. J Neurosci 33: 16459-16470.
    • (2013) J Neurosci , vol.33 , pp. 16459-16470
    • Pinheiro, P.S.1    De Wit, H.2    Walter, A.M.3    Groffen, A.J.4    Verhage, M.5
  • 35
    • 0035924595 scopus 로고    scopus 로고
    • Calmodulin mediates rapid recruitment of fast-releasing synaptic vesicles at a calyx-type synapse
    • Sakaba T, Neher E, (2001) Calmodulin mediates rapid recruitment of fast-releasing synaptic vesicles at a calyx-type synapse. Neuron 32: 1119-1131.
    • (2001) Neuron , vol.32 , pp. 1119-1131
    • Sakaba, T.1    Neher, E.2
  • 36
    • 69449108209 scopus 로고    scopus 로고
    • Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes
    • de Wit H, Walter AM, Milosevic I, Gulyas-Kovacs A, Riedel D, et al. (2009) Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes. Cell 138: 935-946.
    • (2009) Cell , vol.138 , pp. 935-946
    • de Wit, H.1    Walter, A.M.2    Milosevic, I.3    Gulyas-Kovacs, A.4    Riedel, D.5
  • 37
    • 33644852285 scopus 로고    scopus 로고
    • Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles
    • Sorensen JB, Wiederhold K, Muller EM, Milosevic I, Nagy G, et al. (2006) Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles. The EMBO journal 25: 955-966.
    • (2006) The EMBO Journal , vol.25 , pp. 955-966
    • Sorensen, J.B.1    Wiederhold, K.2    Muller, E.M.3    Milosevic, I.4    Nagy, G.5
  • 38
    • 77957198819 scopus 로고    scopus 로고
    • Two distinct secretory vesicle-priming steps in adrenal chromaffin cells
    • Liu Y, Schirra C, Edelmann L, Matti U, Rhee J, et al. (2010) Two distinct secretory vesicle-priming steps in adrenal chromaffin cells. J Cell Biol 190: 1067-1077.
    • (2010) J Cell Biol , vol.190 , pp. 1067-1077
    • Liu, Y.1    Schirra, C.2    Edelmann, L.3    Matti, U.4    Rhee, J.5
  • 39
    • 4043075637 scopus 로고    scopus 로고
    • Calmodulin and Munc13 form a Ca2+ sensor/effector complex that controls short-term synaptic plasticity
    • Junge HJ, Rhee JS, Jahn O, Varoqueaux F, Spiess J, et al. (2004) Calmodulin and Munc13 form a Ca2+ sensor/effector complex that controls short-term synaptic plasticity. Cell 118: 389-401.
    • (2004) Cell , vol.118 , pp. 389-401
    • Junge, H.J.1    Rhee, J.S.2    Jahn, O.3    Varoqueaux, F.4    Spiess, J.5
  • 40
    • 84868688514 scopus 로고    scopus 로고
    • Nonconserved Ca(2+)/calmodulin binding sites in Munc13s differentially control synaptic short-term plasticity
    • Lipstein N, Schaks S, Dimova K, Kalkhof S, Ihling C, et al. (2012) Nonconserved Ca(2+)/calmodulin binding sites in Munc13s differentially control synaptic short-term plasticity. Mol Cell Biol 32: 4628-4641.
    • (2012) Mol Cell Biol , vol.32 , pp. 4628-4641
    • Lipstein, N.1    Schaks, S.2    Dimova, K.3    Kalkhof, S.4    Ihling, C.5
  • 41
    • 0030611081 scopus 로고    scopus 로고
    • Novel Ca2+-binding protein (CAPS) related to UNC-31 required for Ca2+-activated exocytosis
    • Ann K, Kowalchyk JA, Loyet KM, Martin TF, (1997) Novel Ca2+-binding protein (CAPS) related to UNC-31 required for Ca2+-activated exocytosis. J Biol Chem 272: 19637-19640.
    • (1997) J Biol Chem , vol.272 , pp. 19637-19640
    • Ann, K.1    Kowalchyk, J.A.2    Loyet, K.M.3    Martin, T.F.4
  • 43
    • 73949139901 scopus 로고    scopus 로고
    • Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
    • Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, et al. (2009) Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proc Natl Acad Sci U S A 106: 20306-20311.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20306-20311
    • Ellena, J.F.1    Liang, B.2    Wiktor, M.3    Stein, A.4    Cafiso, D.S.5
  • 44
    • 77954366490 scopus 로고    scopus 로고
    • A coiled coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex
    • Wiederhold K, Kloepper TH, Walter AM, Stein A, Kienle N, et al. (2010) A coiled coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex. J Biol Chem 285: 21549-21559.
    • (2010) J Biol Chem , vol.285 , pp. 21549-21559
    • Wiederhold, K.1    Kloepper, T.H.2    Walter, A.M.3    Stein, A.4    Kienle, N.5
  • 46
    • 84864878312 scopus 로고    scopus 로고
    • Complexin arrests a pool of docked vesicles for fast Ca(2+)-dependent release
    • Malsam J, Parisotto D, Bharat TA, Scheutzow A, Krause JM, et al. (2012) Complexin arrests a pool of docked vesicles for fast Ca(2+)-dependent release. The EMBO journal 31: 3270-3281.
    • (2012) The EMBO Journal , vol.31 , pp. 3270-3281
    • Malsam, J.1    Parisotto, D.2    Bharat, T.A.3    Scheutzow, A.4    Krause, J.M.5
  • 47
    • 84863065893 scopus 로고    scopus 로고
    • Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion
    • Wang Z, Liu H, Gu Y, Chapman ER, (2011) Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion. The Journal of cell biology 195: 1159-1170.
    • (2011) The Journal of Cell Biology , vol.195 , pp. 1159-1170
    • Wang, Z.1    Liu, H.2    Gu, Y.3    Chapman, E.R.4
  • 48
    • 33646800207 scopus 로고    scopus 로고
    • Genetic analysis of synaptotagmin 2 in spontaneous and Ca2+-triggered neurotransmitter release
    • Pang ZP, Sun J, Rizo J, Maximov A, Sudhof TC, (2006) Genetic analysis of synaptotagmin 2 in spontaneous and Ca2+-triggered neurotransmitter release. The EMBO journal 25: 2039-2050.
    • (2006) The EMBO Journal , vol.25 , pp. 2039-2050
    • Pang, Z.P.1    Sun, J.2    Rizo, J.3    Maximov, A.4    Sudhof, T.C.5
  • 53
    • 80155205418 scopus 로고    scopus 로고
    • Doc2 is a ca(2+) sensor required for asynchronous neurotransmitter release
    • Yao J, Gaffaney JD, Kwon SE, Chapman ER, (2011) Doc2 is a ca(2+) sensor required for asynchronous neurotransmitter release. Cell 147: 666-677.
    • (2011) Cell , vol.147 , pp. 666-677
    • Yao, J.1    Gaffaney, J.D.2    Kwon, S.E.3    Chapman, E.R.4
  • 54
    • 78049238166 scopus 로고    scopus 로고
    • SNARE protein recycling by alphaSNAP and betaSNAP supports synaptic vesicle priming
    • Burgalossi A, Jung S, Meyer G, Jockusch WJ, Jahn O, et al. (2010) SNARE protein recycling by alphaSNAP and betaSNAP supports synaptic vesicle priming. Neuron 68: 473-487.
    • (2010) Neuron , vol.68 , pp. 473-487
    • Burgalossi, A.1    Jung, S.2    Meyer, G.3    Jockusch, W.J.4    Jahn, O.5
  • 56
    • 0032008553 scopus 로고    scopus 로고
    • Vesicle pools and Ca2+ microdomains: new tools for understanding their roles in neurotransmitter release
    • Neher E, (1998) Vesicle pools and Ca2+ microdomains: new tools for understanding their roles in neurotransmitter release. Neuron 20: 389-399.
    • (1998) Neuron , vol.20 , pp. 389-399
    • Neher, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.