Synaptic vesicle exocytosis

Cold Spring Harb Perspect Biol. 2011 Dec 1;3(12):a005637. doi: 10.1101/cshperspect.a005637.

Abstract

Presynaptic nerve terminals release neurotransmitters by synaptic vesicle exocytosis. Membrane fusion mediating synaptic exocytosis and other intracellular membrane traffic is affected by a universal machinery that includes SNARE (for "soluble NSF-attachment protein receptor") and SM (for "Sec1/Munc18-like") proteins. During fusion, vesicular and target SNARE proteins assemble into an α-helical trans-SNARE complex that forces the two membranes tightly together, and SM proteins likely wrap around assembling trans-SNARE complexes to catalyze membrane fusion. After fusion, SNARE complexes are dissociated by the ATPase NSF (for "N-ethylmaleimide sensitive factor"). Fusion-competent conformations of SNARE proteins are maintained by chaperone complexes composed of CSPα, Hsc70, and SGT, and by nonenzymatically acting synuclein chaperones; dysfunction of these chaperones results in neurodegeneration. The synaptic membrane-fusion machinery is controlled by synaptotagmin, and additionally regulated by a presynaptic protein matrix (the "active zone") that includes Munc13 and RIM proteins as central components.

Publication types

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

MeSH terms

  • Animals
  • Exocytosis*
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / metabolism
  • GTP-Binding Proteins / physiology
  • Humans
  • Membrane Fusion
  • Mice
  • Models, Biological
  • Munc18 Proteins / metabolism
  • Munc18 Proteins / physiology
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Nerve Tissue Proteins / physiology
  • Neurotransmitter Agents / metabolism
  • Protein Folding
  • SNARE Proteins / metabolism
  • SNARE Proteins / physiology
  • Synaptic Vesicles / physiology*
  • Synaptotagmins / metabolism
  • Synaptotagmins / physiology

Substances

  • Munc18 Proteins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • Rim protein, mammalian
  • SNARE Proteins
  • Synaptotagmins
  • GTP-Binding Proteins