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Structure, diversity and synaptic localization of inhibitory glycine receptors.

Betz, H. and Kuhse, J. and Fischer, M. and Schmieden, V. and Laube, Bodo and Kuryatov, A. and Langosch, D. and Meyer, G. and Bormann, J. and Rundström, N. (1994):
Structure, diversity and synaptic localization of inhibitory glycine receptors.
In: Journal of physiology, Paris, pp. 243-8, 88, (4), ISSN 0928-4257, [Article]

Abstract

The inhibitory glycine receptor (GlyR) mediates postsynaptic inhibition in spinal cord, brain stem and other regions of the vertebrate central nervous system. Biochemical and molecular approaches have identified different developmentally and regionally regulated GlyR isoforms that result from the differential expression of at least four genes coding for different variants of the ligand-binding alpha subunit. Molecular studies have allowed identification of GlyR subunit domains implicated in ligand binding, channel formation and receptor assembly. At the postsynaptic membrane, the GlyR colocalizes with a 93-kDa tubulin-binding peripheral membrane protein, gephyrin. Antisense inhibition of gephyrin expression prevents GlyR accumulation at postsynaptic membrane specialization. Thus, gephyrin is essential for postsynaptic receptor topology.

Item Type: Article
Erschienen: 1994
Creators: Betz, H. and Kuhse, J. and Fischer, M. and Schmieden, V. and Laube, Bodo and Kuryatov, A. and Langosch, D. and Meyer, G. and Bormann, J. and Rundström, N.
Title: Structure, diversity and synaptic localization of inhibitory glycine receptors.
Language: English
Abstract:

The inhibitory glycine receptor (GlyR) mediates postsynaptic inhibition in spinal cord, brain stem and other regions of the vertebrate central nervous system. Biochemical and molecular approaches have identified different developmentally and regionally regulated GlyR isoforms that result from the differential expression of at least four genes coding for different variants of the ligand-binding alpha subunit. Molecular studies have allowed identification of GlyR subunit domains implicated in ligand binding, channel formation and receptor assembly. At the postsynaptic membrane, the GlyR colocalizes with a 93-kDa tubulin-binding peripheral membrane protein, gephyrin. Antisense inhibition of gephyrin expression prevents GlyR accumulation at postsynaptic membrane specialization. Thus, gephyrin is essential for postsynaptic receptor topology.

Journal or Publication Title: Journal of physiology, Paris
Volume: 88
Number: 4
Divisions: 10 Department of Biology
10 Department of Biology > Neurophysiology and Neurosensory Systems
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Date Deposited: 12 Apr 2011 11:24
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