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Molecular organization and dynamics of the melatonin MT(1) receptor/RGS20/G(i) protein complex reveal asymmetry of receptor dimers for RGS and G(i) coupling
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SYSNO ASEP 0347607 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Molecular organization and dynamics of the melatonin MT(1) receptor/RGS20/G(i) protein complex reveal asymmetry of receptor dimers for RGS and G(i) coupling Author(s) Maurice, P. (FR)
Daulat, A. M. (FR)
Tureček, Rostislav (UEM-P) RID, ORCID
Ivankova-Susankova, K. (CH)
Zamponi, F. (FR)
Kamal, M. (FR)
Clement, N. (FR)
Guillaume, J. L. (FR)
Bettler, B. (CH)
Galés, C. (FR)
Delagrange, P. (FR)
Jockers, R. (FR)Source Title EMBO Journal. - : Wiley - ISSN 0261-4189
Roč. 29, č. 21 (2010), s. 3646-3659Number of pages 14 s. Language eng - English Country GB - United Kingdom Keywords G protein ; heterodimerization ; molecular organization Subject RIV FH - Neurology R&D Projects GA309/06/1304 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50390512 - UEM-P (2005-2011) UT WOS 000285386700006 DOI 10.1038/emboj.2010.236 Annotation We characterized the molecular complex of the melatonin MT(1) receptor, which couples to G(i) proteins and the regulator of G-protein signalling (RGS) 20. We proposed a model wherein one G(i) and one RGS20 protein bind to separate protomers of MT(1) dimers in a pre-associated complex that rearranges upon agonist activation. 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. Workplace Institute of Experimental Medicine Contact Lenka Koželská, lenka.kozelska@iem.cas.cz, Tel.: 241 062 218, 296 442 218 Year of Publishing 2011
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