IUPHAR/BPS Guide to Pharmacology CITE
https://doi.org/10.2218/gtopdb/F75/2019.4

Ionotropic glutamate receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database



Bernhard Bettler1, Graham L. Collingridge2, Ray Dingledine3, Stephen F. Heinemann4, Michael Hollmann5, Juan Lerma6, David Lodge2, Mark Mayer7, Masayoshi Mishina8, Christophe Mulle9, Shigetada Nakanishi10, Richard Olsen11, Stephane Peineau2, John A. Peters12, Peter Seeburg13, Michael Spedding14 and Jeffrey C. Watkins2
  1. University of Basel, Switzerland
  2. University of Bristol, UK
  3. Emory University, USA
  4. Salk Institute, USA
  5. Ruhr University Bochum, Germany
  6. Universidad Miguel Hernández, Spain
  7. National Institutes of Health, USA
  8. University of Tokyo, Japan
  9. Université Bordeaux 2, France
  10. Kyoto University Faculty of Medicine, Japan
  11. University of California Los Angels, USA
  12. University of Dundee, UK
  13. Max Planck Institute for Medical Research, Germany
  14. Spedding Research Solutions SARL, France


Abstract

The ionotropic glutamate receptors comprise members of the NMDA (N-methyl-D-aspartate), AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid) and kainate receptor classes, named originally according to their preferred, synthetic, agonist [34, 87, 147]. Receptor heterogeneity within each class arises from the homo-oligomeric, or hetero-oligomeric, assembly of distinct subunits into cation-selective tetramers. Each subunit of the tetrameric complex comprises an extracellular amino terminal domain (ATD), an extracellular ligand binding domain (LBD), three transmembrane domains composed of three membrane spans (M1, M3 and M4), a channel lining re-entrant ‘p-loop’ (M2) located between M1 and M3 and an intracellular carboxy- terminal domain (CTD) [94, 66, 102, 147, 77]. The X-ray structure of a homomeric ionotropic glutamate receptor (GluA2 – see below) has recently been solved at 3.6Å resolution [135] and although providing the most complete structural information current available may not representative of the subunit arrangement of, for example, the heteromeric NMDA receptors [69]. It is beyond the scope of this supplement to discuss the pharmacology of individual ionotropic glutamate receptor isoforms in detail; such information can be gleaned from [34, 65, 30, 73, 41, 108, 23, 64, 147, 106, 107, 152]. Agents that discriminate between subunit isoforms are, where appropriate, noted in the tables and additional compounds that distinguish between receptor isoforms are indicated in the text below.

The classification of glutamate receptor subunits has been re-addressed by NC-IUPHAR [27]. The scheme developed recommends a nomenclature for ionotropic glutamate receptor subunits that is adopted here.

NMDA receptors
NMDA receptors assemble as obligate heteromers that may be drawn from GluN1, GluN2A, GluN2B, GluN2C, GluN2D, GluN3A and GluN3B subunits. Alternative splicing can generate eight isoforms of GluN1 with differing pharmacological properties. Various splice variants of GluN2B, 2C, 2D and GluN3A have also been reported. Activation of NMDA receptors containing GluN1 and GluN2 subunits requires the binding of two agonists, glutamate to the S1 and S2 regions of the GluN2 subunit and glycine to S1 and S2 regions of the GluN1 subunit [40, 24]. The minimal requirement for efficient functional expression of NMDA receptors in vitro is a di-heteromeric assembly of GluN1 and at least one GluN2 subunit variant, as a dimer of heterodimers arrangement in the extracellular domain [47, 94, 69]. However, more complex tri-heteromeric assemblies, incorporating multiple subtypes of GluN2 subunit, or GluN3 subunits, can be generated in vitro and occur in vivo. The NMDA receptor channel commonly has a high relative permeability to Ca2+ and is blocked, in a voltage-dependent manner, by Mg2+ such that at resting potentials the response is substantially inhibited.

AMPA and Kainate receptors
AMPA receptors assemble as homomers, or heteromers, that may be drawn from GluA1, GluA2, GluA3 and GluA4 subunits. Transmembrane AMPA receptor regulatory proteins (TARPs) of class I (i.e. γ2, γ3, γ4 and γ8) act, with variable stoichiometry, as auxiliary subunits to AMPA receptors and influence their trafficking, single channel conductance gating and pharmacology (reviewed in [42, 98, 145, 63]). Functional kainate receptors can be expressed as homomers of GluK1, GluK2 or GluK3 subunits. GluK1-3 subunits are also capable of assembling into heterotetramers (e.g. GluK1/K2; [82, 113, 112]). Two additional kainate receptor subunits, GluK4 and GluK5, when expressed individually, form high affinity binding sites for kainate, but lack function, but can form heteromers when expressed with GluK1-3 subunits (e.g. GluK2/K5; reviewed in [113, 64, 112]). Kainate receptors may also exhibit ‘metabotropic’ functions [82, 123]. As found for AMPA receptors, kainate receptors are modulated by auxiliary subunits (Neto proteins, [112, 83]). An important function difference between AMPA and kainate receptors is that the latter require extracellular Na+ and Cl- for their activation [11, 114]. RNA encoding the GluA2 subunit undergoes extensive RNA editing in which the codon encoding a p-loop glutamine residue (Q) is converted to one encoding arginine (R). This Q/R site strongly influences the biophysical properties of the receptor. Recombinant AMPA receptors lacking RNA edited GluA2 subunits are: (1) permeable to Ca2+; (2) blocked by intracellular polyamines at depolarized potentials causing inward rectification (the latter being reduced by TARPs); (3) blocked by extracellular argiotoxin and Joro spider toxins and (4) demonstrate higher channel conductances than receptors containing the edited form of GluA2 [131, 62]. GluK1 and GluK2, but not other kainate receptor subunits, are similarly edited and broadly similar functional characteristics apply to kainate receptors lacking either an RNA edited GluK1, or GluK2, subunit [82, 112]. Native AMPA and kainate receptors displaying differential channel conductances, Ca2+ permeabilites and sensitivity to block by intracellular polyamines have been identified [29, 62, 86]. GluA1-4 can exist as two variants generated by alternative splicing (termed ‘flip’ and ‘flop’) that differ in their desensitization kinetics and their desensitization in the presence of cyclothiazide which stabilises the nondesensitized state. TARPs also stabilise the non-desensitized conformation of AMPA receptors and facilitate the action of cyclothiazide [98]. Splice variants of GluK1-3 also exist which affects their trafficking [82, 112].

Contents

This is a citation summary for Ionotropic glutamate receptors in the Guide to Pharmacology database (GtoPdb). It exists purely as an adjunct to the database to facilitate the recognition of citations to and from the database by citation analyzers. Readers will almost certainly want to visit the relevant sections of the database which are given here under database links.

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Database links

Ionotropic glutamate receptors
http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=75
    Channels and Subunits
            GluA1
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=444
            GluA2
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=445
            GluA3
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=446
            GluA4
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=447
            GluD1
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=448
            GluD2
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=449
            GluK1
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=450
            GluK2
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=451
            GluK3
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=452
            GluK4
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=453
            GluK5
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=454
            GluN1
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=455
            GluN2A
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=456
            GluN2B
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=457
            GluN2C
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=458
            GluN2D
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=459
            GluN3A
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=460
            GluN3B
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=461

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