The molecular machinery of synaptic vesicle exocytosis

Cell Mol Life Sci. 2003 May;60(5):942-60. doi: 10.1007/s00018-003-2240-7.

Abstract

At the synapse, neurotransmitters are released via Ca(2+)-triggered exocytotic fusion of synaptic vesicles with the presynaptic plasma membrane. Synaptic vesicle exocytosis seems to share many basic principles and homologous proteins with other membrane fusion events. Conserved components of the general fusion machinery that participate in synaptic vesicle exocytosis include soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), ATPase N-ethylmaleimide-sensitive factor, Munc18/nSec1, Rab3 GTPase, and the exocyst proteins. In addition, synaptic vesicle exocytosis uses a set of unique components, such as synaptotagmin, complexin, Munc13, and RIM, to meet the special needs of fast Ca(2+)-triggered neurotransmitter release. This review summarizes present knowledge about the molecular mechanisms by which these components mediate and/or regulate synaptic vesicle exocytosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Calcium-Binding Proteins*
  • Exocytosis / physiology*
  • GTP-Binding Proteins*
  • Humans
  • Membrane Fusion
  • Membrane Glycoproteins / physiology
  • Membrane Proteins / physiology
  • Munc18 Proteins
  • Nerve Tissue Proteins / physiology
  • Protein Transport
  • SNARE Proteins
  • Synaptic Vesicles / metabolism*
  • Synaptotagmins
  • Vesicular Transport Proteins / physiology
  • rab3 GTP-Binding Proteins / physiology

Substances

  • Calcium-Binding Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Munc18 Proteins
  • Nerve Tissue Proteins
  • RIMS1 protein, human
  • Rim protein, mammalian
  • Rims1 protein, rat
  • SNARE Proteins
  • UNC13B protein, human
  • Vesicular Transport Proteins
  • Synaptotagmins
  • GTP-Binding Proteins
  • rab3 GTP-Binding Proteins