Postsynaptic receptor scaffold proteins play an important role for concentrating receptor molecules in postsynaptic membranes of central nervous system synapses. In particular, clustering of glycine receptors and different types of GABAA-receptors depends on the scaffold protein gephyrin, which is thought to anchor these receptors to the cytoskeleton. Eukaryotic elongation factor 1A (eEF1A) is a component of the protein synthesis machinery. In addition, it binds and bundles actin and was shown to interact with microtubules. Therefore, it might be involved in regulating the cytoskeletal dynamics in neurons and thereby modulate receptor cluster formation and/or maintenance. In this study, we demonstrate partial colocalization of gephyrin and F-actin along filamentous structures in rat hippocampal neurons. Overexpression of eEF1A in cultured hippocampal neurons results in a significant increase in number, size and density of postsynaptic gephyrin clusters after 21 days in vitro. These findings suggest that eEF1A contributes to the morphology of postsynaptic membrane specializations at inhibitory synapses.