Synaptic vesicle fusion

Nat Struct Mol Biol. 2008 Jul;15(7):665-74. doi: 10.1038/nsmb.1450.


The core of the neurotransmitter release machinery is formed by SNARE complexes, which bring the vesicle and plasma membranes together and are key for fusion, and by Munc18-1, which controls SNARE-complex formation and may also have a direct role in fusion. In addition, SNARE complex assembly is likely orchestrated by Munc13s and RIMs, active-zone proteins that function in vesicle priming and diverse forms of presynaptic plasticity. Synaptotagmin-1 mediates triggering of release by Ca2+, probably through interactions with SNAREs and both membranes, as well as through a tight interplay with complexins. Elucidation of the release mechanism will require a full understanding of the network of interactions among all these proteins and the membranes.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Membrane Fusion / physiology*
  • Munc18 Proteins / chemistry
  • Munc18 Proteins / metabolism
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • SNARE Proteins / chemistry
  • SNARE Proteins / metabolism
  • Synaptic Vesicles / metabolism*
  • Synaptotagmin I / chemistry
  • Synaptotagmin I / metabolism


  • Munc18 Proteins
  • Nerve Tissue Proteins
  • SNARE Proteins
  • Synaptotagmin I