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Mol Cell Neurosci. 2006 Feb;31(2):376-86. Epub 2006 Jan 11.

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

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Department of Neurochemistry, Max-Planck Institute for Brain Research, 60528 Frankfurt, Germany.


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.

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