The oligomeric state sets GABA(B) receptor signalling efficacy

Comps-Agrar, Laëtitia and Kniazeff, Julie and Nørskov-Lauritsen, Lenea and Maurel, Damien and Gassmann, Martin and Gregor, Nathalie and Prézeau, Laurent and Bettler, Bernhard and Durroux, Thierry and Trinquet, Eric and Pin, Jean-Philippe. (2011) The oligomeric state sets GABA(B) receptor signalling efficacy. The EMBO journal, Vol. 30, H. 12. pp. 2336-2349.

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Official URL: http://edoc.unibas.ch/dok/A5844211

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G protein-coupled receptors (GPCRs) have key roles in cell-cell communication. Recent data suggest that these receptors can form large complexes, a possibility expected to expand the complexity of this regulatory system. Among the brain GPCRs, the heterodimeric GABA(B) receptor is one of the most abundant, being distributed in most brain regions, on either pre- or post-synaptic elements. Here, using specific antibodies labelled with time-resolved FRET compatible fluorophores, we provide evidence that the heterodimeric GABA(B) receptor can form higher-ordered oligomers in the brain, as suggested by the close proximity of the GABA(B1) subunits. Destabilizing the oligomers using a competitor or a GABA(B1) mutant revealed different G protein coupling efficiencies depending on the oligomeric state of the receptor. By examining, in heterologous system, the G protein coupling properties of such GABA(B) receptor oligomers composed of a wild-type and a non-functional mutant heterodimer, we provide evidence for a negative functional cooperativity between the GABA(B) heterodimers.
Faculties and Departments:03 Faculty of Medicine > Departement Biomedizin > Division of Physiology > Molecular Neurobiology Synaptic Plasticity (Bettler)
UniBasel Contributors:Bettler, Bernhard
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:10 Apr 2015 09:13
Deposited On:08 Jun 2012 06:40

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