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Molecular Structure and Function of the Glycine Receptor Chloride Channel
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 α-subunits (α1 to α4) and one β-subunit have been identified. The differential expression of subunits underlies a diversity in GlyR pharmacology. A developmental switch from α2 to α1β is completed by around postnatal day 20 in the rat. The β-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 GlyR molecular structure and function. Most of the information has been obtained from homomeric α1 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.
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Cites
The Glutamate Receptor Ion Channels
Dingledine, R., Borges, K., Bowie, D., & Traynelis, S. F. (1999) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01394-2 · Cited by 3,554
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Sites of alcohol and volatile anaesthetic action on GABAA and glycine receptors
Mihic, S. J., Ye, Q., Wick, M. J., Koltchine, V. V., Krasowski, M. D., Finn, S. E., Mascia, M. P., Valenzuela, C. F., Hanson, K. K., Greenblatt, E. P., et al. (1997) · Nature · doi:10.1038/38738 · Cited by 1,219
General anaesthetic actions on ligand-gated ion channels
Krasowski, M. D., & Harrison, N. L. (1999) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180050371 · Cited by 384
Wilson, G. G., & Karlin, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1241 · Cited by 138
Akk, G., Bracamontes, J., & Steinbach, J. H. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.0673e.x · Cited by 137
Cited by
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Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
Rorsman, P., & Ashcroft, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00008.2017 · Cited by 793
Dalmau, J., Geis, C., & Graus, F. (2017) · Physiological Reviews · doi:10.1152/physrev.00010.2016 · Cited by 628
Molecular Targets of Cannabidiol in Neurological Disorders
Ibeas Bih, C., Chen, T., Nunn, A. V. W., Bazelot, M., Dallas, M., & Whalley, B. J. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0377-3 · Cited by 578
Gao, R., & Penzes, P. (2015) · Current Molecular Medicine · doi:10.2174/1566524015666150303003028 · Cited by 516
Carvajal-González, A., Leite, M. I., Waters, P., Woodhall, M., Coutinho, E., Balint, B., Lang, B., Pettingill, P., Carr, A., Sheerin, U.-M., et al. (2014) · Brain · doi:10.1093/brain/awu142 · Cited by 532
Chloride channels as drug targets
Verkman, A. S., & Galietta, L. J. V. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2780 · Cited by 469
Molecular Targets for Antiepileptic Drug Development
Meldrum, B. S., & Rogawski, M. A. (2007) · Neurotherapeutics · doi:10.1016/j.nurt.2006.11.010 · Cited by 468
Glycine receptor mechanism elucidated by electron cryo-microscopy
Du, J., Lü, W., Wu, S., Cheng, Y., & Gouaux, E. (2015) · Nature · doi:10.1038/nature14853 · Cited by 408
Synaptopathies: synaptic dysfunction in neurological disorders – A review from students to students
Lepeta, K., Lourenco, M. V., Schweitzer, B. C., Martino Adami, P. V., Banerjee, P., Catuara‐Solarz, S., de La Fuente Revenga, M., Guillem, A. M., Haidar, M., Ijomone, O. M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13713 · Cited by 386
Native glycine receptor subtypes and their physiological roles
Lynch, J. W. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.07.034 · Cited by 377
Self-citationGlycine transporters: essential regulators of neurotransmission
Eulenburg, V., Armsen, W., Betz, H., & Gomeza, J. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.04.004 · Cited by 327
Zhao, W.-Q., & Townsend, M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.014 · Cited by 291
Glycine receptors: recent insights into their structural organization and functional diversity
Betz, H., & Laube, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03908.x · Cited by 288
Cannabinoids suppress inflammatory and neuropathic pain by targeting α3 glycine receptors
Xiong, W., Cui, T., Cheng, K., Yang, F., Chen, S.-R., Willenbring, D., Guan, Y., Pan, H.-L., Ren, K., Xu, Y., et al. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20120242 · Cited by 288
Layden, M. J., Boekhout, M., & Martindale, M. Q. (2012) · Development · doi:10.1242/dev.073221 · Cited by 98
Yan-Do, R., Duong, E., Manning Fox, J. E., Dai, X., Suzuki, K., Khan, S., Bautista, A., Ferdaoussi, M., Lyon, J., Wu, X., et al. (2016) · Diabetes · doi:10.2337/db15-1272 · Cited by 82
Pest Control Agents from Natural Products
Ujváry, I. (2010) · Hayes' Handbook of Pesticide Toxicology · doi:10.1016/b978-0-12-374367-1.00003-3 · Cited by 81
Shang, Y., Wang, H., Mercaldo, V., Li, X., Chen, T., & Zhuo, M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06314.x · Cited by 72
Baer, K. (2009) · Frontiers in Molecular Neuroscience · doi:10.3389/neuro.02.025.2009 · Cited by 69
Sites of alcohol and volatile anesthetic action on glycine receptors
Lobo, I. A., & Harris, R. A. (2005) · International Review of Neurobiology · doi:10.1016/s0074-7742(04)65003-3 · Cited by 40
Presynaptic control of inhibitory neurotransmitter content in VIAAT containing synaptic vesicles
Aubrey, K. R. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.06.002 · Cited by 30
Koch (2014) · doi:10.1074/jbc.m113.504860 · Cited by 25
Developmental Formation of the GABAergic and Glycinergic Networks in the Mouse Spinal Cord
Shimizu-Okabe, C., Kobayashi, S., Kim, J., Kosaka, Y., Sunagawa, M., Okabe, A., & Takayama, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020834 · Cited by 22
Milestone Review: Unlocking the Proteomics of Glycine Receptor Complexes
Fraser, S. D., Klaassen, R. V., Villmann, C., Smit, A. B., & Harvey, R. J. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70061 · Cited by 10
Genome-wide meta-analysis dissects the genetic basis and health implications of circulating taurine
Zhou, S., Tan, J., Li, X., Ran, Z., He, J., Li, Y., Yuan, X., Hu, Y., Chen, M., Dai, Y., et al. (2026) · Functional & Integrative Genomics · doi:10.1007/s10142-026-02067-9
Metadata
- Authors
- Lynch, J. W.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2004-10
- Volume
- 84
- Issue
- 4
- Pages
- 1051-1095
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2021842829
- Cited by
- 778
- References
- 6
- FWCI
- 2.26
- Type
- journal article
- Language
- en
- Open access
- closed
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