Complexins: small but capable

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• 作者：Ralf Mohrmann ; Madhurima Dhara ; Dieter Bruns
• 关键词：Complexin ; Synaptotagmin ; SNARE regulators ; Membrane fusion ; Ca2+ triggered exocytosis
• 刊名：Cellular and Molecular Life Sciences (CMLS)
• 出版年：2015
• 出版时间：November 2015
• 年：2015
• 卷：72
• 期：22
• 页码：4221-4235
• 全文大小：899 KB
• 参考文献：1.Wickner W, Schekman R (2008) Membrane fusion. Nat Struct Mol Biol 15:658-64PubMedCentral PubMed
  2.Sudhof TC, Rothman JE (2009) Membrane fusion: grappling with SNARE and SM proteins. Science 323:474-77PubMedCentral PubMed
  3.Jahn R, Fasshauer D (2012) Molecular machines governing exocytosis of synaptic vesicles. Nature 490:201-07PubMedCentral PubMed
  4.Fasshauer D, Sutton RB, Brunger AT, Jahn R (1998) Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci USA 95:15781-5786PubMedCentral PubMed
  5.Sutton RB, Fasshauer D, Jahn R, Brunger AT (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395:347-53PubMed
  6.Fasshauer D, Otto H, Eliason WK, Jahn R, Brunger AT (1997) Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. J Biol Chem 272:28036-8041PubMed
  7.Fiebig KM, Rice LM, Pollock E, Brunger AT (1999) Folding intermediates of SNARE complex assembly. Nat Struct Biol 6:117-23PubMed
  8.Chen YA, Scales SJ, Scheller RH (2001) Sequential SNARE assembly underlies priming and triggering of exocytosis. Neuron 30:161-70PubMed
  9.Sorensen JB, Wiederhold K, Muller EM, Milosevic I, Nagy G, de Groot BL, Grubmuller H, Fasshauer D (2006) Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles. EMBO J 25:955-66PubMedCentral PubMed
  10.Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998) SNAREpins: minimal machinery for membrane fusion. Cell 92:759-72PubMed
  11.Wojcik SM, Brose N (2007) Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter. Neuron 55:11-4PubMed
  12.Sudhof TC (2013) Neurotransmitter release: the last millisecond in the life of a synaptic vesicle. Neuron 80:675-90PubMed
  13.van den Bogaart G, Thutupalli S, Risselada JH, Meyenberg K, Holt M, Riedel D, Diederichsen U, Herminghaus S, Grubmuller H, Jahn R (2011) Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation. Nat Struct Mol Biol 18:U805–U882
  14.Gao Y, Zorman S, Gundersen G, Xi Z, Ma L, Sirinakis G, Rothman JE, Zhang Y (2012) Single reconstituted neuronal SNARE complexes zipper in three distinct stages. Science 337:1340-343PubMedCentral PubMed
  15.Zorman S, Rebane AA, Ma L, Yang G, Molski MA, Coleman J, Pincet F, Rothman JE, Zhang Y (2014) Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins. eLife 3:e03348PubMedCentral PubMed
  16.Ishizuka T, Saisu H, Odani S, Abe T (1995) Synaphin: a protein associated with the docking/fusion complex in presynaptic terminals. Biochem Biophys Res Commun 213:1107-114PubMed
  17.McMahon HT, Missler M, Li C, Sudhof TC (1995) Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 83:111-19PubMed
  18.Reim K, Wegmeyer H, Brandstatter JH, Xue M, Rosenmund C, Dresbach T, Hofmann K, Brose N (2005) Structurally and functionally unique complexins at retinal ribbon synapses. J Cell Biol 169:669-80PubMedCentral PubMed
  19.Buhl LK, Jorquera RA, Akbergenova Y, Huntwork-Rodriguez S, Volfson D, Littleton JT (2013) Differential regulation of evoked and spontaneous neurotransmitter release by C-terminal modifications of complexin. Mol Cell Neurosci 52:161-72PubMedCentral PubMed
  20.Pabst S, Hazzard JW, Antonin W, Sudhof TC, Jahn R, Rizo J, Fasshauer D (2000) Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. J Biol Chem 275:19808-9818PubMed
  21.Chen X, Tomchick DR, Kovrigin E, Arac D, Machius M, Sudhof TC, Rizo J (2002) Three-dimensional structure of the complexin/SNARE complex. Neuron 33:397-09PubMed
  22.Weninger K, Bowen ME, Choi UB, Chu S, Brunger AT (2008) Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16:308-20PubMedCentral PubMed
  23.Pabst S, Margittai M, Vainius D, Langen R, Jahn R, Fasshauer D (2002) Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. J Biol Chem 277:7838-848PubMed
  24.Bowen ME, Weninger K, Ernst J, Chu S, Brunger AT (2005) Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex. Biophys J 89:690-02PubMedCentral PubMed
  25.Li Y, Augustine GJ, Weninger K (2007) Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events. Biophys J 93:2178-187PubMedCentral PubMed
  26.Hu K, Carroll J, Rickman C, Davletov B (2002) Action of complexin on SNARE complex. J Biol Chem 277:41652-1656PubMed
  27.Bracher A, Kadlec J, Betz H, Weissenhorn W (2002) X-Ray structure of a neuronal complexin-SNARE complex from squid. J Biol Chem 277:26517-6523PubMed <
• 作者单位：Ralf Mohrmann (1) (2)
  Madhurima Dhara (2)
  Dieter Bruns (2)
  
  1. Zentrum für Human- und Molekularbiologie, University of Saarland, CIPMM, 66421, Homburg/Saar, Germany
  2. Medical Faculty, Department of Physiology, University of Saarland, CIPMM, 66421, Homburg/Saar, Germany
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Cell Biology
  Biomedicine
  Life Sciences
  Biochemistry
  
• 出版者：Birkh盲user Basel
• ISSN：1420-9071

文摘

Despite intensive research, it is still unclear how an immediate and profound acceleration of exocytosis is triggered by appropriate Ca2+-stimuli in presynaptic terminals. This is due to the fact that the molecular mechanisms of “docking-and “priming-reactions, which set up secretory vesicles to fuse at millisecond time scale, are extremely hard to study. Yet, driven by a fruitful combination of in vitro and in vivo analyses, our mechanistic understanding of Ca2+-triggered vesicle fusion has certainly advanced in the past few years. In this review, we aim to highlight recent progress and emerging views on the molecular mechanisms, by which constitutively forming SNAREpins are organized in functional, tightly regulated units for synchronized release. In particular, we will focus on the role of the small regulatory factor complexin whose function in Ca2+-dependent exocytosis has been controversially discussed for more than a decade. Special emphasis will also be laid on the functional relationship of complexin and synaptotagmin, as both proteins possibly act as allies and/or antagonists to govern SNARE-mediated exocytosis. Keywords Complexin Synaptotagmin SNARE regulators Membrane fusion Ca2+ triggered exocytosis