4.5 Review Book Chapter

Molecular Mechanisms of Fast Neurotransmitter Release

Journal

ANNUAL REVIEW OF BIOPHYSICS, VOL 47
Volume 47, Issue -, Pages 469-497

Publisher

ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-070816-034117

Keywords

synaptic vesicle fusion; fusion protein; action potential; synaptic vesicle priming; Ca2+ triggering

Categories

Funding

  1. NATIONAL INSTITUTE OF MENTAL HEALTH [K99MH113764, R37MH063105] Funding Source: NIH RePORTER
  2. NATIONAL INSTITUTE ON AGING [P50AG047366] Funding Source: NIH RePORTER
  3. Howard Hughes Medical Institute Funding Source: Medline
  4. NIA NIH HHS [P50 AG047366] Funding Source: Medline
  5. NIMH NIH HHS [R37 MH063105, R00 MH113764, K99 MH113764] Funding Source: Medline

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This review summarizes current knowledge of synaptic proteins that are central to synaptic vesicle fusion in presynaptic active zones, including SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptors), synaptotagmin, complexin, Munc18 (mammalian uncoordinated-18), and Munc13 (mammalian uncoordinated-13), and highlights recent insights in the cooperation of these proteins for neurotransmitter release. Structural and functional studies of the synaptic fusion machinery suggest new molecular models of synaptic vesicle priming and Ca2+-triggered fusion. These studies will be a stepping-stone toward answering the question of how the synaptic vesicle fusion machinery achieves such high speed and sensitivity.

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