The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex

Abstract

Significant progress has been made towards the identification of functional domains of the inhibitory glycine receptor. Several residues crucial for ligand binding, ion-channel properties and stoichiometric subunit assembly have been identified. A major recent advance has been the finding that the biogenesis of postsynaptic glycine receptor clusters requires the tubulin-binding protein, gephyrin. Another area of exciting research has focused on mutations of glycine receptor alpha and beta subunit genes, which have been found to be causal for different hereditary motor disorders.