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Volumn 45, Issue 4, 2010, Pages 389-397

Comparative analysis of Drosophila and mammalian complexins as fusion clamps and facilitators of neurotransmitter release

Author keywords

Exocytosis; Neurotransmitter release; SNARE complex; Synapse; Synaptic vesicle

Indexed keywords

COMPLEXIN; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 77957936989     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2010.07.012     Document Type: Article
Times cited : (58)

References (36)
  • 1
    • 70449733048 scopus 로고    scopus 로고
    • Postsynaptic regulation of synaptic plasticity by synaptotagmin 4 requires both C2 domains
    • Barber C.F., Jorquera R.A., Melom J.E., Littleton J.T. Postsynaptic regulation of synaptic plasticity by synaptotagmin 4 requires both C2 domains. J. Cell Biol. 2009, 187:295-310.
    • (2009) J. Cell Biol. , vol.187 , pp. 295-310
    • Barber, C.F.1    Jorquera, R.A.2    Melom, J.E.3    Littleton, J.T.4
  • 2
    • 0037135615 scopus 로고    scopus 로고
    • X-ray structure of a neuronal complexin-SNARE complex from squid
    • Bracher A., Kadlec J., Betz H., Weissenhorn W. X-ray structure of a neuronal complexin-SNARE complex from squid. J. Biol. Chem. 2002, 277:26517-26523.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26517-26523
    • Bracher, A.1    Kadlec, J.2    Betz, H.3    Weissenhorn, W.4
  • 3
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand A.H., Perrimon N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 1993, 118:401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 4
    • 49749126732 scopus 로고    scopus 로고
    • For better or for worse: complexins regulate SNARE function and vesicle fusion
    • Brose N. For better or for worse: complexins regulate SNARE function and vesicle fusion. Traffic 2008, 9:1403-1413.
    • (2008) Traffic , vol.9 , pp. 1403-1413
    • Brose, N.1
  • 7
    • 0028061861 scopus 로고
    • Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse
    • Geppert M., Goda Y., Hammer R.E., Li C., Rosahl T.W., Stevens C.F., Sudhof T.C. Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse. Cell 1994, 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    Stevens, C.F.6    Sudhof, T.C.7
  • 8
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • Giraudo C.G., Eng W.S., Melia T.J., Rothman J.E. A clamping mechanism involved in SNARE-dependent exocytosis. Science 2006, 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
  • 11
    • 34748846347 scopus 로고    scopus 로고
    • A complexin fusion clamp regulates spontaneous neurotransmitter release and synaptic growth
    • Huntwork S., Littleton J.T. A complexin fusion clamp regulates spontaneous neurotransmitter release and synaptic growth. Nat. Neurosci. 2007, 10:1235-1237.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1235-1237
    • Huntwork, S.1    Littleton, J.T.2
  • 13
    • 0027249801 scopus 로고
    • Expression of synaptotagmin in Drosophila reveals transport and localization of synaptic vesicles to the synapse
    • Littleton J.T., Bellen H.J., Perin M.S. Expression of synaptotagmin in Drosophila reveals transport and localization of synaptic vesicles to the synapse. Development 1993, 118:1077-1088.
    • (1993) Development , vol.118 , pp. 1077-1088
    • Littleton, J.T.1    Bellen, H.J.2    Perin, M.S.3
  • 14
    • 0032142949 scopus 로고    scopus 로고
    • Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly
    • Littleton J.T., Chapman E.R., Kreber R., Garment M.B., Carlson S.D., Ganetzky B. Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Neuron 1998, 21:401-413.
    • (1998) Neuron , vol.21 , pp. 401-413
    • Littleton, J.T.1    Chapman, E.R.2    Kreber, R.3    Garment, M.B.4    Carlson, S.D.5    Ganetzky, B.6
  • 16
    • 58849164361 scopus 로고    scopus 로고
    • Complexin controls the force transfer from SNARE complexes to membranes in fusion
    • Maximov A., Tang J., Yang X., Pang Z.P., Sudhof T.C. Complexin controls the force transfer from SNARE complexes to membranes in fusion. Science 2009, 323:516-521.
    • (2009) Science , vol.323 , pp. 516-521
    • Maximov, A.1    Tang, J.2    Yang, X.3    Pang, Z.P.4    Sudhof, T.C.5
  • 17
    • 0028880456 scopus 로고
    • Complexins: cytosolic proteins that regulate SNAP receptor function
    • McMahon H.T., Missler M., Li C., Sudhof T.C. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 1995, 83:111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Sudhof, T.C.4
  • 19
    • 0034733545 scopus 로고    scopus 로고
    • Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions
    • Pabst S., Hazzard J.W., Antonin W., Sudhof T.C., Jahn R., Rizo J., Fasshauer D. Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. J. Biol. Chem. 2000, 275:19808-19818.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19808-19818
    • Pabst, S.1    Hazzard, J.W.2    Antonin, W.3    Sudhof, T.C.4    Jahn, R.5    Rizo, J.6    Fasshauer, D.7
  • 20
    • 18244408224 scopus 로고    scopus 로고
    • Kinetics of exocytosis is faster in cones than in rods
    • Rabl K., Cadetti L., Thoreson W.B. Kinetics of exocytosis is faster in cones than in rods. J. Neurosci. 2005, 25:4633-4640.
    • (2005) J. Neurosci. , vol.25 , pp. 4633-4640
    • Rabl, K.1    Cadetti, L.2    Thoreson, W.B.3
  • 21
    • 77957969859 scopus 로고    scopus 로고
    • Image J. U. S. National Institutes of Health, Bethesda, MD, 2009
    • Rasband, W.S., 1997-2009. Image J. U. S. National Institutes of Health, Bethesda, MD, http://rsb.info.nih.gov/ij/.
    • (1997)
    • Rasband, W.S.1
  • 25
    • 67650161468 scopus 로고    scopus 로고
    • A role of complexin-lipid interactions in membrane fusion
    • Seiler F., Malsam J., Krause J.M., Sollner T.H. A role of complexin-lipid interactions in membrane fusion. FEBS Lett. 2009, 583:2343-2348.
    • (2009) FEBS Lett. , vol.583 , pp. 2343-2348
    • Seiler, F.1    Malsam, J.2    Krause, J.M.3    Sollner, T.H.4
  • 26
    • 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 M.K., Whiteheart S.W., Scheller R.H., Rothman J.E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 1993, 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
  • 29
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J., Maximov A., Shin O.H., Dai H., Rizo J., Sudhof T.C. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 2006, 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    Sudhof, T.C.6
  • 30
    • 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 T.C. Synaptotagmin-1, -2, and -9: Ca(2+) sensors for fast release that specify distinct presynaptic properties in subsets of neurons. Neuron 2007, 54:567-581.
    • (2007) Neuron , vol.54 , pp. 567-581
    • Xu, J.1    Mashimo, T.2    Sudhof, T.C.3
  • 31
    • 77951975523 scopus 로고    scopus 로고
    • Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity
    • Xue M., Craig T.K., Xu J., Chao H.T., Rizo J., Rosenmund C. Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity. Nat. Struct. Mol. Biol. 2010, 17:568-575.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 568-575
    • Xue, M.1    Craig, T.K.2    Xu, J.3    Chao, H.T.4    Rizo, J.5    Rosenmund, C.6
  • 32
    • 70350772355 scopus 로고    scopus 로고
    • Tilting the balance between facilitatory and inhibitory functions of mammalian and Drosophila Complexins orchestrates synaptic vesicle exocytosis
    • Xue M., Lin Y.Q., Pan H., Reim K., Deng H., Bellen H.J., Rosenmund C. Tilting the balance between facilitatory and inhibitory functions of mammalian and Drosophila Complexins orchestrates synaptic vesicle exocytosis. Neuron 2009, 64:367-380.
    • (2009) Neuron , vol.64 , pp. 367-380
    • Xue, M.1    Lin, Y.Q.2    Pan, H.3    Reim, K.4    Deng, H.5    Bellen, H.J.6    Rosenmund, C.7
  • 34
    • 45549089944 scopus 로고    scopus 로고
    • Complexins facilitate neurotransmitter release at excitatory and inhibitory synapses in mammalian central nervous system
    • Xue M., Stradomska A., Chen H., Brose N., Zhang W., Rosenmund C., Reim K. Complexins facilitate neurotransmitter release at excitatory and inhibitory synapses in mammalian central nervous system. Proc. Natl Acad. Sci. USA 2008, 105:7875-7880.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7875-7880
    • Xue, M.1    Stradomska, A.2    Chen, H.3    Brose, N.4    Zhang, W.5    Rosenmund, C.6    Reim, K.7
  • 35
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara M., Littleton J.T. Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release. Neuron 2002, 36:897-908.
    • (2002) Neuron , vol.36 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2
  • 36
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: molecular mechanisms and functional consequences
    • Zhang F.L., Casey P.J. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 1996, 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.