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G‐protein‐coupled receptor oligomers: two or more for what? Lessons from mGlu and GABA B receptors
Author(s) -
Pin J.P.,
CompsAgrar L.,
Maurel D.,
Monnier C.,
Rives M. L.,
Trinquet E.,
Kniazeff J.,
Rondard P.,
Prézeau L.
Publication year - 2009
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2009.179978
Subject(s) - metabotropic receptor , rhodopsin like receptors , receptor , g protein coupled receptor , class c gpcr , metabotropic glutamate receptor , gabab receptor , glutamate receptor , metabotropic glutamate receptor 6 , biology , microbiology and biotechnology , long term depression , neuroscience , chemistry , biochemistry , gabaa receptor , ampa receptor
G‐protein‐coupled receptors (GPCRs) are key players in the precise tuning of intercellullar communication. In the brain, both major neurotransmitters, glutamate and GABA, act on specific GPCRs [the metabotropic glutamate (mGlu) and GABA B receptors] to modulate synaptic transmission. These receptors are encoded by the largest gene family, and have been found to associate into both homo‐ and hetero‐oligomers, which increases the complexity of this cell communication system. Here we show that dimerization is required for mGlu and GABA B receptors to function, since the activation process requires a relative movement between the subunits to occur. We will also show that, in contrast to the mGlu receptors, which form strict dimers, the GABA B receptors assemble into larger complexes, both in transfected cells and in the brain, resulting in a decreased G‐protein coupling efficacy. We propose that GABA B receptor oligomerization offers a way to increase the possibility of modulating receptor signalling and activity, allowing the same receptor protein to have specific properties in neurons at different locations.