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The beta-adrenergic receptor kinase interacts with the amino terminus of the G protein beta subunit.
Goldman, P S; DeMaggio, A J; Hoekstra, M F; Goodman, R H.
Afiliación
  • Goldman PS; Vollum Institute, Oregon Health Sciences University, Portland 97201, USA. goldmanp@ohsu.edu
Biochem Biophys Res Commun ; 240(2): 425-9, 1997 Nov 17.
Article en En | MEDLINE | ID: mdl-9388495
Desensitization of G protein-coupled receptors involves phosphorylation of the receptors by G protein-coupled receptor kinases, such as the beta-adrenergic 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 carboxyl 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.
Asunto(s)
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Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Quinasas Dependientes de AMP Cíclico / Proteínas de Unión al GTP Límite: Animals Idioma: En Revista: Biochem Biophys Res Commun Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos
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Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Quinasas Dependientes de AMP Cíclico / Proteínas de Unión al GTP Límite: Animals Idioma: En Revista: Biochem Biophys Res Commun Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos