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Molecular organization and dynamics of the melatonin MT ? receptor/RGS20/G(i) protein complex reveal asymmetry of receptor dimers for RGS and G(i) coupling

Maurice, Pascal and Daulat, Avais M. and Turecek, Rostislav and Ivankova-Susankova, Klara and Zamponi, Francesco and Kamal, Maud and Clement, Nathalie and Guillaume, Jean-Luc and Bettler, Bernhard and Galès, Céline and Delagrange, Philippe and Jockers, Ralf. (2010) Molecular organization and dynamics of the melatonin MT ? receptor/RGS20/G(i) protein complex reveal asymmetry of receptor dimers for RGS and G(i) coupling. The EMBO journal, Vol. 29, H. 21. pp. 3646-3659.

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Official URL: http://edoc.unibas.ch/dok/A6005286

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Abstract

Functional asymmetry of G-protein-coupled receptor (GPCR) dimers has been reported for an increasing number of cases, but the molecular architecture of signalling units associated to these dimers remains unclear. Here, we characterized the molecular complex of the melatonin MT ? receptor, which directly and constitutively couples to G(i) proteins and the regulator of G-protein signalling (RGS) 20. The molecular organization of the ternary MT ?/G(i)/RGS20 complex was monitored in its basal and activated state by bioluminescence resonance energy transfer between probes inserted at multiple sites of the complex. On the basis of the reported crystal structures of G(i) and the RGS domain, we propose a model wherein one G(i) and one RGS20 protein bind to separate protomers of MT ? dimers in a pre-associated complex that rearranges upon agonist activation. This model was further validated with MT ?/MT heterodimers. Collectively, our data extend the concept of asymmetry within GPCR dimers, reinforce the notion of receptor specificity for RGS proteins and highlight the advantage of GPCRs organized as dimers in which each protomer fulfils its specific task by binding to different GPCR-interacting proteins.
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
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:0261-4189
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Nov 2012 16:23
Deposited On:08 Nov 2012 16:19

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