IUPHAR/BPS Guide to Pharmacology CITE
https://doi.org/10.2218/gtopdb/F40/2023.1

Metabotropic glutamate receptors in GtoPdb v.2023.1



Francine Acher1, Giuseppe Battaglia2, Hans Bräuner-Osborne3, P. Jeffrey Conn4, Robert Duvoisin5, Francesco Ferraguti6, Peter J. Flor7, Cyril Goudet8, Karen J. Gregory9, David Hampson10, Michael P. Johnson11, Yoshihiro Kubo12, James Monn13, Shigetada Nakanishi14, Ferdinando Nicoletti15, Colleen Niswender4, Jean-Philippe Pin8, Philippe Rondard8, Darryle D. Schoepp11, Ryuichi Shigemoto16 and Michihiro Tateyama12
  1. Université René Descarte, France
  2. IRCCS NEUROMED, Italy
  3. University of Copenhagen, Denmark
  4. Vanderbilt University, USA
  5. Oregon Health & Science University, USA
  6. Innsbruck University, Austria
  7. Novartis Institutes for Biomedical Research, Switzerland
  8. Université de Montpellier, France
  9. Monash University, Australia
  10. University of Toronto, Canada
  11. Lilly Research Laboratories, USA
  12. National Institute for Physiological Sciences, Japan
  13. Eli Lilly and Company, USA
  14. Kyoto University Faculty of Medicine, Japan
  15. University of Rome 'La Sapienza', Italy
  16. Institute of Science and Technology, Austria


Abstract

Metabotropic glutamate (mGlu) receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on Metabotropic Glutamate Receptors [351]) are a family of G protein-coupled receptors activated by the neurotransmitter glutamate [140]. The mGlu family is composed of eight members (named mGlu1 to mGlu8) which are divided in three groups based on similarities of agonist pharmacology, primary sequence and G protein coupling to effector: Group-I (mGlu1 and mGlu5), Group-II (mGlu2 and mGlu3) and Group-III (mGlu4, mGlu6, mGlu7 and mGlu8) (see Further reading).

Structurally, mGlu are composed of three juxtaposed domains: a core G protein-activating seven-transmembrane domain (TM), common to all GPCRs, is linked via a rigid cysteine-rich domain (CRD) to the Venus Flytrap domain (VFTD), a large bi-lobed extracellular domain where glutamate binds. mGlu form constitutive dimers, cross-linked by a disulfide bridge. The structures of the VFTD of mGlu1, mGlu2, mGlu3, mGlu5 and mGlu7 have been solved [200, 275, 268, 403]. The structure of the 7 transmembrane (TM) domains of both mGlu1 and mGlu5 have been solved, and confirm a general helical organisation similar to that of other GPCRs, although the helices appear more compacted [88, 433, 62]. Recent advances in cryo-electron microscopy have provided structures of full-length mGlu receptor homodimers [217, 191] and heterodimers [91]. Studies have revealed the possible formation of heterodimers between either group-I receptors, or within and between group-II and -III receptors [89]. First characterised in transfected cells, co-localisation and specific pharmacological properties suggest the existence of such heterodimers in the brain [270, 440, 145, 283, 259, 218]. Beyond heteromerisation with other mGlu receptor subtypes, increasing evidence suggests mGlu receptors form heteromers and larger order complexes with class A GPCRs (reviewed in [140]).

The endogenous ligands of mGlu are L-glutamic acid, L-serine-O-phosphate, N-acetylaspartylglutamate (NAAG) and L-cysteine sulphinic acid. Group-I mGlu receptors may be activated by 3,5-DHPG and (S)-3HPG [30] and antagonised by (S)-hexylhomoibotenic acid [235]. Group-II mGlu receptors may be activated by LY389795 [269], LY379268 [269], eglumegad [354, 434], DCG-IV and (2R,3R)-APDC [355], and antagonised by eGlu [170] and LY307452 [425, 105]. Group-III mGlu receptors may be activated by L-AP4 and (R,S)-4-PPG [130]. An example of an antagonist selective for mGlu receptors is LY341495, which blocks mGlu2 and mGlu3 at low nanomolar concentrations, mGlu8 at high nanomolar concentrations, and mGlu4, mGlu5, and mGlu7 in the micromolar range [185]. In addition to orthosteric ligands that directly interact with the glutamate recognition site, allosteric modulators that bind within the TM domain have been described. Negative allosteric modulators are listed separately. The positive allosteric modulators most often act as ‘potentiators’ of an orthosteric agonist response, without significantly activating the receptor in the absence of agonist.

Contents

This is a citation summary for Metabotropic 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.

GtoPdb is an expert-driven guide to pharmacological targets and the substances that act on them. GtoPdb is a reference work which is most usefully represented as an on-line database. As in any publication this work should be appropriately cited, and the papers it cites should also be recognized. This document provides a citation for the relevant parts of the database, and also provides a reference list for the research cited by those parts. For further details see [42].

Please note that the database version for the citations given in GtoPdb are to the most recent preceding version in which the family or its subfamilies and targets were substantially changed. The links below are to the current version. If you need to consult the cited version, rather than the most recent version, please contact the GtoPdb curators.

Database links

Metabotropic glutamate receptors
https://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=40
Introduction to Metabotropic glutamate receptors
https://www.guidetopharmacology.org/GRAC/FamilyIntroductionForward?familyId=40
    Receptors
            mGlu1 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=289
            mGlu2 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=290
            mGlu3 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=291
            mGlu4 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=292
            mGlu5 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=293
            mGlu6 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=294
            mGlu7 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=295
            mGlu8 receptor
            https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=296

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