Počet záznamů: 1

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

  1. 1.
    0347607 - UEM-P 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
    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

    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