Ps. Goldman et al., THE BETA-ADRENERGIC-RECEPTOR KINASE INTERACTS WITH THE AMINO-TERMINUSOF THE G-PROTEIN BETA-SUBUNIT, Biochemical and biophysical research communications, 240(2), 1997, pp. 425-429
Desensitization of G protein-coupled receptors involves phosphorylatio
n of the receptors by G protein-coupled receptor kinases, such as the
beta-adrenerse receptor kinase (beta ARK). beta ARK activity depends u
pon its translocation from the cytoplasm to the membrane. The beta gam
ma subunits of G proteins bind to beta ARK and recruit the kinase to t
he membrane. The G beta gamma binding domain is localized to a carboyl
terminal region of beta ARK but the beta ARK binding domain of G beta
gamma is not known, We used the yeast two-hybrid assay to characteriz
e the interaction between G beta and beta ARK. We demonstrate an inter
action between the carboxyl terminus of beta ARK and G beta 2. The str
ength of this interaction is increased when the VP16 transactivation d
omain is placed on the carboxyl end of G beta(2), indicating that an a
ccessible G beta 2 amino terminus is important for its interaction wit
h beta ARK. In addition, we show that amino acids 1 to 145 of G beta 2
are sufficient for beta ARK binding. (C) 1997 Academic Press.