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

Synaptic vesicle exocytosis.

Author information

1
Department of Molecular and Cellular Physiology, and Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California 94305, USA. tcs1@stanford.edu

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.

PMID:
22026965
PMCID:
PMC3225952
DOI:
10.1101/cshperspect.a005637
[Indexed for MEDLINE]
Free PMC Article

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