Cited by 263Neuroscience and Neuropharmacology ResearchAmino Acid Enzymes and MetabolismReceptor Mechanisms and Signaling

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Influence of GluN2 subunit identity on NMDA receptor function

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Wyllie, D.J.A., Livesey, M.R., Hardingham, G.E.·2013·Neuropharmacology

DOI 10.1016/j.neuropharm.2013.01.016PMC PMC3778433

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Abstract

N-methyl-d-aspartate receptors (NMDARs) are ligand-gated ion channels ('ionotropic' receptors) activated by the major excitatory neurotransmitter, l-glutamate. While the term 'the NMDAR' is often used it obscures the fact that this class of receptor contains within it members whose properties are as different as they are similar. This heterogeneity was evident from early electrophysiological, pharmacological and biochemical assessments of the functional properties of NMDARs and while the molecular basis of this heterogeneity has taken many years to elucidate, it indicated from the outset that the diversity of NMDAR phenotypes could allow this receptor family to subserve a variety of functions in the mammalian central nervous system. In this review we highlight some recent studies that have identified structural elements within GluN2 subunits that contribute to the heterogeneous biophysical properties of NMDARs, consider why some recently described novel pharmacological tools may permit better identification of native NMDAR subtypes, examine the evidence that NMDAR subtypes differentially contribute to the induction of long-term potentiation and long-term depression and discuss how through the use of chimeric proteins additional insights have been obtained that account for NMDAR subtype-dependency of physiological and pathophysiological signalling. This article is part of the Special Issue entitled 'Glutamate Receptor-Dependent Synaptic Plasticity'.

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Authors: Wyllie, D. J. A., Livesey, M. R., & Hardingham, G. E.
Affiliations: University of Edinburgh (GB)
Corresponding author: Wyllie, D.J.A.
ORCID: Wyllie, D.J.A.
Livesey, M.R.
Hardingham, G.E.
Venue: Neuropharmacology
Publisher: Elsevier BV
Published: 2013-11
Volume: 74
Pages: 4-17
ISSN: 0028-3908 (ISSN-L)
DOI: 10.1016/j.neuropharm.2013.01.016
PMC: PMC3778433
OpenAlex: W2108909652
Cited by: 260
References: 161
Citations by year: 2026: 6 · 2025: 27 · 2024: 21 · 2023: 16 · 2022: 29 · 2021: 24 · 2020: 20 · 2019: 23 · 2018: 26 · 2017: 18 · 2016: 18 · 2015: 16 · 2014: 10 · 2013: 5
FWCI: 1.66
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/3.0/ (vor)
Locations: Neuropharmacology (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
Funders: The Wellcome Trust
The Medical Research Council
The Biotechnology and Biological Science Research Council
The European Union
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: NMDA receptor, GluN2 subunits, receptor heterogeneity, ionotropic glutamate receptors, receptor subtypes, long-term potentiation, long-term depression, synaptic plasticity, fusion protein, receptor pharmacology, glutamate signalling
MeSH terms: Animals, Models, Molecular, Neuronal Plasticity, Receptors, N-Methyl-D-Aspartate, Long-Term Potentiation, Excitatory Amino Acid Antagonists, Protein Subunits, Protein Multimerization

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Influence of GluN2 subunit identity on NMDA receptor function

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