Premium
Active Gα q subunits and M3 acetylcholine receptors promote distinct modes of association of RGS2 with the plasma membrane
Author(s) -
Clark Michael A.,
Sethi Pooja R.,
Lambert Nevin A.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.045
Subject(s) - heterotrimeric g protein , rgs2 , fluorescence recovery after photobleaching , chemistry , g protein , membrane protein , microbiology and biotechnology , biophysics , gtpase , gtpase activating protein , membrane , receptor , biochemistry , biology
RGS proteins accelerate the GTPase activity of heterotrimeric G proteins at the plasma membrane. Association of RGS proteins with the plasma membrane can be mediated by interactions with other membrane proteins and by direct interactions with the lipid bilayer. Here we use fluorescence recovery after photobleaching (FRAP) to characterize interactions between RGS2 and M3 acetylcholine receptors (M3Rs), Gα subunits and the lipid bilayer. Active Gα q and M3Rs both recruited RGS2‐EGFP to the plasma membrane. RGS2‐EGFP remained bound to the plasma membrane between interactions with active Gα q , but rapidly exchanged between membrane‐associated and cytosolic pools when recruited by M3Rs.