Cited by 3,568Neuroscience and Neuropharmacology ResearchNicotinic Acetylcholine Receptors StudyReceptor Mechanisms and Signaling

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Glutamate Receptor Ion Channels: Structure, Regulation, and Function

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Traynelis, Stephen F., Wollmuth, Lonnie P., McBain, Chris J., Menniti, Frank S., Vance, Katie M., Ogden, Kevin K., Hansen, Kasper B., Yuan, Hongjie, Myers, Scott J., Dingledine, Ray·2010·Pharmacological Reviews

DOI 10.1124/pr.109.002451PMC PMC2964903

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Abstract

The mammalian ionotropic glutamate receptor family encodes 18 gene products that coassemble to form ligand-gated ion channels containing an agonist recognition site, a transmembrane ion permeation pathway, and gating elements that couple agonist-induced conformational changes to the opening or closing of the permeation pore. Glutamate receptors mediate fast excitatory synaptic transmission in the central nervous system and are localized on neuronal and non-neuronal cells. These receptors regulate a broad spectrum of processes in the brain, spinal cord, retina, and peripheral nervous system. Glutamate receptors are postulated to play important roles in numerous neurological diseases and have attracted intense scrutiny. The description of glutamate receptor structure, including its transmembrane elements, reveals a complex assembly of multiple semiautonomous extracellular domains linked to a pore-forming element with striking resemblance to an inverted potassium channel. In this review we discuss International Union of Basic and Clinical Pharmacology glutamate receptor nomenclature, structure, assembly, accessory subunits, interacting proteins, gene expression and translation, post-translational modifications, agonist and antagonist pharmacology, allosteric modulation, mechanisms of gating and permeation, roles in normal physiological function, as well as the potential therapeutic use of pharmacological agents acting at glutamate receptors.

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8 of the 1399 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

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Sorted by citations

NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease
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“Moreover, the particular glutamate receptor genes prioritized by DEPICT ( GRIK3 , GRM1 , GRM5 , and GRM8 ) suggest the importance of processes involving communication between neurons on an intermediate time scale 18,19 , such as learning and memory.”

See all 3,568

Authors: Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., & Dingledine, R.
Affiliations: Emory University (US)
ORCID: Traynelis, Stephen F.
Wollmuth, Lonnie P.
McBain, Chris J.
Menniti, Frank S.
Ogden, Kevin K.
Hansen, Kasper B.
Yuan, Hongjie
Myers, Scott J.
Venue: Pharmacological Reviews
Publisher: Elsevier BV
Published: 2010-09
Volume: 62
Issue: 3
Pages: 405-496
ISSN: 0031-6997 (ISSN-L)
DOI: 10.1124/pr.109.002451
PMC: PMC2964903
OpenAlex: W2037852973
Cited by: 3,568
References: 1,399
Citations by year: 2026: 151 · 2025: 181 · 2024: 216 · 2023: 201 · 2022: 247 · 2021: 279 · 2020: 269 · 2019: 272 · 2018: 235 · 2017: 268 · 2016: 242 · 2015: 221 · 2014: 257 · 2013: 221 · 2012: 162
FWCI: 15.66
Type: journal article
Language: en
Update notices: erratum (2014-10-01)
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Pharmacological Reviews (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Michael J. Fox Foundation for Parkinson's Research
Lundbeckfonden
H. Lundbeck A/S
National Institutes of Health (NS036654)
National Institute of Mental Health (MH066892, R01MH066892)
National Institute on Drug Abuse (T32-DA01504006, T32DA015040)
National Eye Institute (R01EY016979, EY01697905)
National Institute of General Medical Sciences (GM008602, T32GM008602)
National Institute of Neurological Disorders and Stroke (R37NS036654, NS036604, NS068464, R01NS065371, NS065371, R01NS036654, NS036654, R01NS068464, R01NS036604)
National Institute of Environmental Health Sciences (T32ES012870)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: ionotropic glutamate receptors, ligand-gated ion channels, receptor structure, receptor assembly, auxiliary subunits, receptor regulation, post-translational modification, allosteric modulation, gating mechanism, ion permeation, excitatory synaptic transmission, receptor nomenclature, neurological disorders, therapeutic agents
MeSH terms: Humans, Ion Channels, Synaptic Transmission, Terminology as Topic, Protein Processing, Post-Translational, Gene Expression, Receptors, Glutamate, Protein Subunits

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Glutamate Receptor Ion Channels: Structure, Regulation, and Function

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