Conformational switch of syntaxin-1 controls synaptic vesicle fusion

Science. 2008 Sep 12;321(5895):1507-10. doi: 10.1126/science.1163174. Epub 2008 Aug 14.

Abstract

During synaptic vesicle fusion, the soluble N-ethylmaleimide-sensitive factor-attachment protein receptor (SNARE) protein syntaxin-1 exhibits two conformations that both bind to Munc18-1: a "closed" conformation outside the SNARE complex and an "open" conformation in the SNARE complex. Although SNARE complexes containing open syntaxin-1 and Munc18-1 are essential for exocytosis, the function of closed syntaxin-1 is unknown. We generated knockin/knockout mice that expressed only open syntaxin-1B. Syntaxin-1B(Open) mice were viable but succumbed to generalized seizures at 2 to 3 months of age. Binding of Munc18-1 to syntaxin-1 was impaired in syntaxin-1B(Open) synapses, and the size of the readily releasable vesicle pool was decreased; however, the rate of synaptic vesicle fusion was dramatically enhanced. Thus, the closed conformation of syntaxin-1 gates the initiation of the synaptic vesicle fusion reaction, which is then mediated by SNARE-complex/Munc18-1 assemblies.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / metabolism
  • Epilepsy / etiology
  • Excitatory Postsynaptic Potentials
  • Membrane Fusion
  • Mice
  • Mice, Knockout
  • Munc18 Proteins / metabolism
  • Mutation
  • Protein Conformation
  • Protein Structure, Tertiary
  • SNARE Proteins / metabolism
  • Sucrose / metabolism
  • Synapses / physiology
  • Synaptic Vesicles / physiology*
  • Synaptic Vesicles / ultrastructure
  • Syntaxin 1 / chemistry*
  • Syntaxin 1 / genetics
  • Syntaxin 1 / metabolism*

Substances

  • Munc18 Proteins
  • SNARE Proteins
  • Syntaxin 1
  • Sucrose
  • Calcium