Molecular structure and function of the glycine receptor chloride channel

Lynch, J. W. (2004) Molecular structure and function of the glycine receptor chloride channel. Physiological Reviews, 84 4: 1051-1095. doi:10.1152/physrev.00042.2003

Author Lynch, J. W.
Title Molecular structure and function of the glycine receptor chloride channel
Journal name Physiological Reviews   Check publisher's open access policy
ISSN 0031-9333
Publication date 2004-10-01
Year available 2004
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1152/physrev.00042.2003
Open Access Status
Volume 84
Issue 4
Start page 1051
End page 1095
Total pages 45
Editor Susan Hamilton
Place of publication Bethesda, MD, USA
Publisher American Physiological Society
Language eng
Subject C1
270601 Animal Physiology - Biophysics
730104 Nervous system and disorders
Abstract The glycine receptor chloride channel (GlyR) is a member of the nicotinic acetylcholine receptor family of ligand-gated ion channels. Functional receptors of this family comprise five subunits and are important targets for neuroactive drugs. The GlyR is best known for mediating inhibitory neurotransmission in the spinal cord and brain stem, although recent evidence suggests it may also have other physiological roles, including excitatory neurotransmission in embryonic neurons. To date, four alpha-subunits (alpha1 to alpha4) and one beta-subunit have been identified. The differential expression of subunits underlies a diversity in GlyR pharmacology. A developmental switch from alpha2 to alpha1beta is completed by around postnatal day 20 in the rat. The beta-subunit is responsible for anchoring GlyRs to the subsynaptic cytoskeleton via the cytoplasmic protein gephyrin. The last few years have seen a surge in interest in these receptors. Consequently, a wealth of information has recently emerged concerning Glyl? molecular structure and function. Most of the information has been obtained from homomeric alpha1 GlyRs, with the roles of the other subunits receiving relatively little attention. Heritable mutations to human GlyR genes give rise to a rare neurological disorder, hyperekplexia (or startle disease). Similar syndromes also occur in other species. A rapidly growing list of compounds has been shown to exert potent modulatory effects on this receptor. Since GlyRs are involved in motor reflex circuits of the spinal cord and provide inhibitory synapses onto pain sensory neurons, these agents may provide lead compounds for the development of muscle relaxant and peripheral analgesic drugs.
Keyword Physiology
Nicotinic Acetylcholine-receptor
Gated Ion Channels
Rat Spinal-cord
Ventral Tegmental Area
Retinal Ganglion-cells
Membrane-spanning Segment
Brain-stem Motoneurons
Q-Index Code C1
Institutional Status UQ
Additional Notes This document is a journal review.

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Excellence in Research Australia (ERA) - Collection
2005 Higher Education Research Data Collection
School of Biomedical Sciences Publications
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Citation counts: TR Web of Science Citation Count  Cited 407 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 445 times in Scopus Article | Citations
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Created: Wed, 15 Aug 2007, 15:21:48 EST