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Structure and functions of inhibitory and excitatory glycine receptors
Journal article   Peer reviewed

Structure and functions of inhibitory and excitatory glycine receptors

H Betz, J Kuhse, V Schmieden, B Laube, J Kirsch and Robert J Harvey
Annals of the New York Academy of Sciences, Vol.868, pp.667-676
1999
url
https://doi.org/10.1111/j.1749-6632.1999.tb11343.xView
Published Version

Abstract

chloride channel excitatory amino acid receptor gephyrin glycine receptor isoprotein receptor subunit zinc ion
The strychnine-sensitive glycine receptor (GlyR) is a pentameric chloride channel protein that exists in several developmentally and regionally regulated isoforms in the CNS. These result from the differential expression of four genes encoding different variants (α1-α4) of the ligand-binding subunit of the GlyR. Their assembly with the structural β subunit is governed by 'assembly cassettes' within the extracellular domains of these proteins and creates chloride channels of distinct conductance properties. GlyR gating is potentiated by Zn2+, a metal ion co-released with different neurotransmitters. Site-directed mutagenesis has unraveled major determinants of agonist binding and Zn(Z+) potentiation. During development, glycine receptors mediate excitation that results in Ca2+ influx and neurotransmitter release. Ca2+ influx triggered by the activation of embryonic GlyRs is required for the synaptic localization of the GlyR and its anchoring protein gepyhrin. In the adult, mutations in GlyR subunit genes result in motor disorders. The spastic and spasmodic phenotypes in mouse as well as human hereditary startle disease will be discussed.

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