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Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Open accessAbstract
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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“NMDARs are heterotetrameric ligand-gated ionotropic receptors”
From Mechanisms of ketamine and its metabolites as antidepressants (2022) · cites this paper as Traynelis et al., 2010
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In the citing paper
“The NMDAR ion channel is heteromeric, composed of two obligatory GluN1 subunits and two GluN2 or GluN3 subunits.”
From Lipid Nanoparticle Delivery of siRNA to Silence Neuronal Gene Expression in the Brain (2013) · cites this paper as [19]
The cited source says what the claim attributes to it.
In the citing paper
“Expression of GluN1 is necessary for the formation of a functional NMDAR channel in the plasma membrane.19”
From Lipid Nanoparticle Delivery of siRNA to Silence Neuronal Gene Expression in the Brain (2013) · cites this paper as [19]
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In the citing paper
“The proposed role of glutamate as a signal molecule in ctenophores is supported by an unprecedented diversity of ionotropic glutamate receptors(iGluRs;ExtendedDataFig.7a,bandSupplementaryTable27)far exceeding the number of genes encoding iGluRs in other basal metazoans 28 .”
From The ctenophore genome and the evolutionary origins of neural systems (2014) · cites this paper as [28]
Experimental — accuracy not yet measuredIn the citing paper
“Throughout the central nervous system, the vast majority of fast synaptic neurotransmission arises via AMPARs (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“The M2 reentrant transmembrane loop of the AMPAR subunit forms the lining of the channel pore, and amino acids in the so-called “QRN” site determine the ion selectivity of the channel (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“Unlike GluA1, GluA3 and GluA4 subunits which contain an unedited glutamine (Q) most GluA2 subunits contain a fully edited arginine (R) at this site which has important consequences for single channel conductance, Ca2+-permeability, and channel block by polyamines (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“Of these subunits, incorporation of GluA2 is key to the overall biophysical properties of the receptor.”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“The TARP family comprises six isoforms, which differentially modify almost every function of native AMPARs (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“As described in section VA, CP-AMPARs are both Ca2+ permeable and blocked in a voltage-dependent manner by cytoplasmic polyamines, such as spermine and spermidine (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“NMDARs typically contain two GluN1 subunits and either two GluN2 subunits or a mixture of GluN2/GluN3 subunits 28, 29.”
From Mechanisms of ketamine action as an antidepressant (2018) · cites this paper as [29]
In the citing paper
“Both immunohistochemical and electrophysiological studies have confirmed the existence of extra-synaptic NMDARs, which are not located in the post-synaptic density 68, and are primarily comprised of GluN2B-containing heterotetramers 28, 29.”
From Mechanisms of ketamine action as an antidepressant (2018) · cites this paper as [29]
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Metadata
- 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
- Venue
- Pharmacological Reviews
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 62
- Issue
- 3
- Pages
- 405-496
- ISSN
- 0031-6997 (ISSN-L)
- 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
- 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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