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

Phyllis S. Goldman, Anthony J. DeMaggio, Merl F. Hoekstra, Richard H. Goodman

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Desensitization of G protein-coupled receptors involves phosphorylation of the receptors by G protein-coupled receptor kinases, such as the β-adrenergic receptor kinase (βARK). βARK activity depends upon its translocation from the cytoplasm to the membrane. The βγ subunits of G proteins bind to βARK and recruit the kinase to the membrane. The Gβγ binding domain is localized to a carboxyl terminal region of βARK but the βARK binding domain of Gβγ is not known. We used the yeast two-hybrid assay to characterize the interaction between Gβ and βARK. We demonstrate an interaction between the carboxyl terminus of βARK and Gβ2. The strength of this interaction is increased when the VP16 transactivation domain is placed on the carboxyl end of Gβ2, indicating that an accessible Gβ2 amino terminus is important for its interaction with βARK. In addition, we show that amino acids 1 to 145 of Gβ2 are sufficient for βARK binding.

Original languageEnglish (US)
Pages (from-to)425-429
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume240
Issue number2
DOIs
StatePublished - Nov 17 1997

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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