Actin-dependent regulation of neurotransmitter release at central synapses

Neuron. 2000 Sep;27(3):539-50. doi: 10.1016/s0896-6273(00)00064-7.

Abstract

Depolymerization of actin by latrunculin A transiently promotes neurotransmitter release. The mean rate of mEPSCs increases by a Ca2+-independent process, without a concomitant change in the mean amplitude. The readily releasable vesicle pool size and the rate of refilling of the readily releasable pool remain unaltered by latrunculin treatment. Evoked neurotransmitter release also increases in a manner consistent with an increase in vesicle release probability. The observed enhancement of neurotransmitter release is specific to actin depolymerization mediated by latrunculin A and is not caused by cytochalasin D. Our findings indicate that actin participates in a regulatory mechanism that restrains fusion of synaptic vesicles at the active zone.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / analysis
  • Actins / drug effects
  • Actins / metabolism*
  • Animals
  • Bridged Bicyclo Compounds, Heterocyclic / metabolism
  • Bridged Bicyclo Compounds, Heterocyclic / pharmacology
  • Calcium / metabolism
  • Cells, Cultured
  • Cytochalasin D / pharmacology
  • Depsipeptides*
  • Egtazic Acid / analogs & derivatives*
  • Excitatory Postsynaptic Potentials
  • Fluorescent Antibody Technique
  • Green Fluorescent Proteins
  • Hippocampus / metabolism*
  • Luminescent Proteins / genetics
  • Marine Toxins / pharmacology
  • Mice
  • Nerve Tissue Proteins / metabolism
  • Neurotransmitter Agents / metabolism*
  • Peptides, Cyclic / pharmacology
  • Presynaptic Terminals / metabolism
  • Rats
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Synapses / metabolism*
  • Synaptic Transmission / drug effects
  • Synaptic Vesicles / metabolism
  • Thiazoles / metabolism
  • Thiazoles / pharmacology
  • Thiazolidines

Substances

  • Actins
  • Bridged Bicyclo Compounds, Heterocyclic
  • Bsn protein, mouse
  • Bsn protein, rat
  • Depsipeptides
  • Luminescent Proteins
  • Marine Toxins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • Peptides, Cyclic
  • Recombinant Fusion Proteins
  • Thiazoles
  • Thiazolidines
  • jasplakinolide
  • Green Fluorescent Proteins
  • Cytochalasin D
  • Egtazic Acid
  • swinholide A
  • 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid
  • latrunculin A
  • Calcium