메뉴 건너뛰기




Volumn 25, Issue 45, 2005, Pages 10546-10555

The role of snapin in neurosecretion: Snapin knock-out mice exhibit impaired calcium-dependent exocytosis of large dense-core vesicles in chromaffin cells

Author keywords

Catecholamine; Chromaffin cell; Exocytosis; Neurosecretion; Snare proteins; Synaptic vesicle release

Indexed keywords

CALCIUM; CATECHOLAMINE; SNAPIN; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNAPTOTAGMIN I; UNCLASSIFIED DRUG;

EID: 27744502972     PISSN: 02706474     EISSN: 02706474     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.3275-05.2005     Document Type: Article
Times cited : (82)

References (38)
  • 2
    • 0035368680 scopus 로고    scopus 로고
    • How does calcium trigger neurotransmitter release?
    • Augustine GJ (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
  • 3
    • 1842475284 scopus 로고    scopus 로고
    • Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions
    • Bai J, Wang CT, Richards DA, Jackson MB, Chapman ER (2004) Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions. Neuron 41:929-942.
    • (2004) Neuron , vol.41 , pp. 929-942
    • Bai, J.1    Wang, C.T.2    Richards, D.A.3    Jackson, M.B.4    Chapman, E.R.5
  • 4
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH (1992) Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257:255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 5
    • 0142138839 scopus 로고    scopus 로고
    • Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells
    • Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T (2003) Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells. Biochem J 375:433-440.
    • (2003) Biochem J , vol.375 , pp. 433-440
    • Buxton, P.1    Zhang, X.M.2    Walsh, B.3    Sriratana, A.4    Schenberg, I.5    Manickam, E.6    Rowe, T.7
  • 6
    • 0028350057 scopus 로고
    • Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking
    • Calakos N, Bennett MK, Peterson K, Scheller RH (1994) Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science 263:1146-1149.
    • (1994) Science , vol.263 , pp. 1146-1149
    • Calakos, N.1    Bennett, M.K.2    Peterson, K.3    Scheller, R.H.4
  • 7
    • 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
  • 9
    • 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
  • 10
    • 4344715395 scopus 로고    scopus 로고
    • Generation and analysis of Brca1 conditional knockout mice
    • Deng CX, Xu X (2004) Generation and analysis of Brca1 conditional knockout mice. Methods Mol Biol 280:185-200.
    • (2004) Methods Mol Biol , vol.280 , pp. 185-200
    • Deng, C.X.1    Xu, X.2
  • 11
    • 0032555126 scopus 로고    scopus 로고
    • Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly
    • Fasshauer D, Eliason WK, Brünger AT, Jahn R (1998) Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry 37:10354-10362.
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1    Eliason, W.K.2    Brünger, A.T.3    Jahn, R.4
  • 13
    • 0033361978 scopus 로고    scopus 로고
    • Coupling calcium to SNARE-mediated synaptic vesicle fusion
    • Hilfiker S, Greengard P, Augustine GJ (1999) Coupling calcium to SNARE-mediated synaptic vesicle fusion. Nat Neurosci 2:104-106.
    • (1999) Nat Neurosci , vol.2 , pp. 104-106
    • Hilfiker, S.1    Greengard, P.2    Augustine, G.J.3
  • 14
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi JM, Mochida S, Sheng ZH (1999) Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat Neurosci 2:119-124.
    • (1999) Nat Neurosci , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 15
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R, Sudhof TC (1999) Membrane fusion and exocytosis. Annu Rev Biochem 68:863-911.
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 16
    • 0037175388 scopus 로고    scopus 로고
    • Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in non-secretory cells
    • Jaiswal JK, Andrews NW, Simon SM (2002) Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in non-secretory cells. J Cell Biol 159:625-635.
    • (2002) J Cell Biol , vol.159 , pp. 625-635
    • Jaiswal, J.K.1    Andrews, N.W.2    Simon, S.M.3
  • 18
    • 2942614748 scopus 로고    scopus 로고
    • Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity
    • Morenilla-Palao C, Planells-Cases R, Garcia-Sanz N, Ferrer-Montiel A (2004) Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity. J Biol Chem 279:25665-25672.
    • (2004) J Biol Chem , vol.279 , pp. 25665-25672
    • Morenilla-Palao, C.1    Planells-Cases, R.2    Garcia-Sanz, N.3    Ferrer-Montiel, A.4
  • 19
    • 0000598955 scopus 로고    scopus 로고
    • Common mechanisms for regulated exocytosis in the chromaffin cell and the synapse
    • Morgan A, Burgoyne RD (1997) Common mechanisms for regulated exocytosis in the chromaffin cell and the synapse. Semin Cell Dev Biol 8:141-149.
    • (1997) Semin Cell Dev Biol , vol.8 , pp. 141-149
    • Morgan, A.1    Burgoyne, R.D.2
  • 20
    • 0032498539 scopus 로고    scopus 로고
    • Fusion of lysosomes with late endosomes produces a hybrid organelle of intermediate density and is NSF dependent
    • Mullock BM, Bright NA, Fearon CW, Gray SR, Luzio JP (1998) Fusion of lysosomes with late endosomes produces a hybrid organelle of intermediate density and is NSF dependent. J Cell Biol 140:591-601.
    • (1998) J Cell Biol , vol.140 , pp. 591-601
    • Mullock, B.M.1    Bright, N.A.2    Fearon, C.W.3    Gray, S.R.4    Luzio, J.P.5
  • 21
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein SNAP-25 differentially expressed by neuronal subpopulations
    • Oyler GA, Higgins GA, Hart RA, Battenberg E, Billingsley M, Bloom FE, Wilson MC (1989) The identification of a novel synaptosomal-associated protein SNAP-25 differentially expressed by neuronal subpopulations. J Cell Biol 109:3039-3052.
    • (1989) J Cell Biol , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 22
    • 0037174660 scopus 로고    scopus 로고
    • 2+-triggered exocytosis
    • 2+-triggered exocytosis. Science 298:781-785.
    • (2002) Science , vol.298 , pp. 781-785
    • Rettig, J.1    Neher, E.2
  • 23
    • 2442584514 scopus 로고    scopus 로고
    • Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis
    • Rao SK, Huynh C, Proux-Gillardeaux V, Galli T, Andrews NW (2004) Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis. J Biol Chem 279:20471-20479.
    • (2004) J Biol Chem , vol.279 , pp. 20471-20479
    • Rao, S.K.1    Huynh, C.2    Proux-Gillardeaux, V.3    Galli, T.4    Andrews, N.W.5
  • 26
    • 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. Pflügers Arch 448:347-362.
    • (2004) Pflügers Arch , vol.448 , pp. 347-362
    • Sorensen, J.B.1
  • 28
  • 30
    • 3142580943 scopus 로고    scopus 로고
    • Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)
    • Starcevic M, Dell'Angelica EC (2004) Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1). J Biol Chem 279:28393-28401.
    • (2004) J Biol Chem , vol.279 , pp. 28393-28401
    • Starcevic, M.1    Dell'Angelica, E.C.2
  • 31
    • 3242747322 scopus 로고    scopus 로고
    • Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons
    • Thakur P, Stevens DR, Sheng ZH, Rettig J (2004) Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons. J Neurosci 24:6476-6481.
    • (2004) J Neurosci , vol.24 , pp. 6476-6481
    • Thakur, P.1    Stevens, D.R.2    Sheng, Z.H.3    Rettig, J.4
  • 32
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble WS, Cowan DM, Scheller RH (1988) VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc Natl Acad Sci USA 85:4538-4542.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 33
    • 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
  • 34
    • 2942750191 scopus 로고    scopus 로고
    • Reinvestigation of the role of snapin in neurotransmitter release
    • Vites O, Rhee JS, Schwarz M, Rosenmund C, Jahn R (2004) Reinvestigation of the role of snapin in neurotransmitter release. J Biol Chem 279:26251-26256.
    • (2004) J Biol Chem , vol.279 , pp. 26251-26256
    • Vites, O.1    Rhee, J.S.2    Schwarz, M.3    Rosenmund, C.4    Jahn, R.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 (2001a) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.