The beta-adrenergic receptor kinase interacts with the amino terminus of the G protein beta subunit

被引:9
作者
Goldman, PS [1 ]
DeMaggio, AJ [1 ]
Hoekstra, MF [1 ]
Goodman, RH [1 ]
机构
[1] ICOS CORP,BOTHELL,WA 98021
关键词
D O I
10.1006/bbrc.1997.7674
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Desensitization of G protein-coupled receptors involves phosphorylation of the receptors by G protein-coupled receptor kinases, such as the beta-adrenerse receptor kinase (beta ARK). beta ARK activity depends upon its translocation from the cytoplasm to the membrane. The beta gamma subunits of G proteins bind to beta ARK and recruit the kinase to the 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 characterize the interaction between G beta and beta ARK. We demonstrate an interaction between the carboxyl terminus of beta ARK and G beta 2. The strength of this interaction is increased when the VP16 transactivation domain is placed on the carboxyl end of G beta(2), indicating that an accessible G beta 2 amino terminus is important for its interaction with 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.
引用
收藏
页码:425 / 429
页数:5
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