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

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.
Mesh Terms:
Actin Cytoskeleton, Actins, Animals, Antineoplastic Agents, Bridged Bicyclo Compounds, Heterocyclic, Carrier Proteins, Cell Adhesion Molecules, Cells, Cultured, Cytochalasin D, Cytoskeleton, Depsipeptides, Hippocampus, Humans, Membrane Proteins, Microfilament Proteins, Neurons, Nucleic Acid Synthesis Inhibitors, Phosphoproteins, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins, Synapses, Thiazoles, Thiazolidines
Mol. Cell. Neurosci.
Date: Feb. 01, 2006
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