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

0347607 - ÚEM 2011 RIV GB eng J - Článek v odborném periodiku
Maurice, P. - Daulat, A. M. - Tureček, Rostislav - Ivankova-Susankova, K. - Zamponi, F. - Kamal, M. - Clement, N. - Guillaume, J. L. - Bettler, B. - Galés, C. - Delagrange, P. - Jockers, R.
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.
EMBO Journal. Roč. 29, č. 21 (2010), s. 3646-3659. ISSN 0261-4189. E-ISSN 1460-2075
Grant CEP: GA ČR GA309/06/1304
Výzkumný záměr: CEZ:AV0Z50390512
Klíčová slova: G protein * heterodimerization * molecular organization
Kód oboru RIV: FH - Neurologie, neurochirurgie, neurovědy
Impakt faktor: 10.124, rok: 2010
http://arl-repository.lib.cas.cz/uloziste_av/UEM-P/cav_un_epca-0347607_01.pdf

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.
Trvalý link: http://hdl.handle.net/11104/0188354