The state of the actin cytoskeleton determines its association with gephyrin: role of ena/VASP family members

Mol Cell Neurosci. 2006 Feb;31(2):376-86. doi: 10.1016/j.mcn.2005.11.004. Epub 2006 Jan 11.

Abstract

The role the cytoskeleton plays in generating and/or maintaining gephyrin-dependent receptor clusters at inhibitory synapses is poorly understood. Here, the effects of actin cytoskeleton disruption were investigated in eGFP-gephyrin-transfected cells and hippocampal neurons. While gephyrin was not associated with microfilaments in transfected cells, it colocalized with G-actin and cytochalasin-D-induced F-actin patches. The linker region between the MoeA and MogA homology domains of gephyrin was required for colocalization with F-actin patches and for the binding of gephyrin to ena/VASP, an actin anti-capping factor that, in vitro, caused gephyrin binding to polymerized actin. In hippocampal neurons, treatment with cytochalasin D resulted in the redistribution of the neuronal ena/VASP homologue Mena into actin patches and, at early stages of development, a reduction in the number of gephyrin clusters. Our data suggest that Mena binding to F-actin allows for gephyrin recruitment to the leading edge of uncapped actin filaments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actins / genetics
  • Actins / metabolism*
  • Animals
  • Antineoplastic Agents / pharmacology
  • Bridged Bicyclo Compounds, Heterocyclic / pharmacology
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Cells, Cultured
  • Cytochalasin D / pharmacology
  • Cytoskeleton / drug effects
  • Cytoskeleton / metabolism*
  • Depsipeptides / pharmacology
  • Hippocampus / cytology
  • Humans
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Neurons / cytology
  • Neurons / metabolism
  • Nucleic Acid Synthesis Inhibitors / pharmacology
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Protein Structure, Tertiary
  • Rats
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Synapses / metabolism
  • Synapses / ultrastructure
  • Thiazoles / pharmacology
  • Thiazolidines

Substances

  • Actins
  • Antineoplastic Agents
  • Bridged Bicyclo Compounds, Heterocyclic
  • Carrier Proteins
  • Cell Adhesion Molecules
  • Depsipeptides
  • Membrane Proteins
  • Microfilament Proteins
  • Nucleic Acid Synthesis Inhibitors
  • Phosphoproteins
  • Recombinant Fusion Proteins
  • Thiazoles
  • Thiazolidines
  • gephyrin
  • vasodilator-stimulated phosphoprotein
  • jasplakinolide
  • Cytochalasin D
  • latrunculin A