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Complexin controls the force transfer from SNARE complexes to membranes in fusion

Academic Article
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Overview

authors

  • Maximov, Anton
  • Tang, J.
  • Yang, X.
  • Pang, Z. P. P.
  • Sudhof, T. C.

publication date

  • January 2009

journal

  • Science  Journal

abstract

  • Trans-SNAP receptor (SNARE, where SNAP is defined as soluble NSF attachment protein, and NSF is defined as N-ethylmaleimide-sensitive factor) complexes catalyze synaptic vesicle fusion and bind complexin, but the function of complexin binding to SNARE complexes remains unclear. Here we show that in neuronal synapses, complexin simultaneously suppressed spontaneous fusion and activated fast calcium ion-evoked fusion. The dual function of complexin required SNARE binding and also involved distinct amino-terminal sequences of complexin that localize to the point where trans-SNARE complexes insert into the fusing membranes, suggesting that complexin controls the force that trans-SNARE complexes apply onto the fusing membranes. Consistent with this hypothesis, a mutation in the membrane insertion sequence of the v-SNARE synaptobrevin/vesicle-associated membrane protein (VAMP) phenocopied the complexin loss-of-function state without impairing complexin binding to SNARE complexes. Thus, complexin probably activates and clamps the force transfer from assembled trans-SNARE complexes onto fusing membranes.

subject areas

  • Action Potentials
  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Animals
  • Calcium
  • Cells, Cultured
  • Excitatory Postsynaptic Potentials
  • Membrane Fusion
  • Mice
  • Mice, Knockout
  • Mutant Proteins
  • Nerve Tissue Proteins
  • Neurons
  • Protein Binding
  • R-SNARE Proteins
  • SNARE Proteins
  • Synapses
  • Synaptic Vesicles
  • Synaptotagmins
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Identity

PubMed Central ID

  • PMC3235366

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1166505

PubMed ID

  • 19164751
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Additional Document Info

start page

  • 516

end page

  • 521

volume

  • 323

issue

  • 5913

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