Delta-Opioid receptors exhibit high efficiency when activating trimeric G proteins in membrane domains

0142563 - FGU-C 20030014 RIV GB eng J - Journal Article
Bouřová, Lenka - Koštrnová, Alexandra - Hejnová, Lucie - Moravcová, Zuzana - Moon, H. E. - Novotný st., Jiří - Milligan, G. - Svoboda, Petr
Delta-Opioid receptors exhibit high efficiency when activating trimeric G proteins in membrane domains.
Journal of Neurochemistry. Roč. 85, č. 1 (2003), s. 34-49. ISSN 0022-3042. E-ISSN 1471-4159
R&D Projects: GA MŠMT LN00A026; GA ČR GA309/01/0255
Grant - others:Welcome Trust(GB) xx
Institutional research plan: CEZ:AV0Z5011922
Keywords : membrane domains * GTPase activity * G protein coupling
Subject RIV: CE - Biochemistry
Impact factor: 4.825, year: 2003

Low-density membrane fragments (domains) were separated from the bulk plasma membranes of HEK293 cells expressing DOP receptor-Gi1alpha fusion protein by drastic homogenization and flotation on sucrose density gradient. Low-density domains exhibited four times higher agonist-stimulated GTPase activity and GTPgammaS binding than the bulk plasma membranes (when corrected for expression levels of the receptor). RGS1 enhanced further the G protein functional activity but did not remove the difference between domain-bound and plasma membrane pools of G protein. By contrast, detergent-extraction of membrane domains diminished functional coupling between G proteinůcoupled receptor and corresponding G protein.
Permanent Link: http://hdl.handle.net/11104/0040264