Summary

GABAergic synapses are the major sites of inhibitory transmission in the brain. The key functional components, GABAa receptors, are GABA-gated chloride channels sensitive to benzodiazepines and barbiturates. Among a wide diversity of subunit compositions, most common is a pentamer of two a1, two P2, and one y 2 subunit. The y 2 subunit contributes to synaptic localization of the complex. Point mutant knock-in mice of individual a subunits revealed specific roles for a1 in sedation and amnesia and a2 in anxiety. Trafficking of GABAA receptors is regulated by interacting proteins and by extracellular signals such as epileptogenic activity. Other key components of GABAergic synapses include cell adhesion complexes of cadherins, and presynaptic neurexins with postsynaptic dystroglycan or neuroligin-2. Recent evidence suggests that neurexins and neuroligins function to recruit components to GABA synapses and to control the balance of GABA and glutamate synapses. A major intracellular postsynaptic component is gephyrin, which anchors some GABAA receptors and may recruit other molecules to the postsynaptic site. Despite recent progress, the molecular linkages among key components such as GABAA receptors, gephyrin, and neuroligins have not been identified, indicating that much is yet to be discovered about the composition and assembly of GABAergic synapses.

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