Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors.


Journal Article

The rate and extent of the agonist-dependent phosphorylation of beta 2-adrenergic receptors and rhodopsin by beta-adrenergic receptor kinase (beta ARK) are markedly enhanced on addition of G protein beta gamma subunits. With a model peptide substrate it was demonstrated that direct activation of the kinase could not account for this effect. G protein beta gamma subunits were shown to interact directly with the COOH-terminal region of beta ARK, and formation of this beta ARK-beta gamma complex resulted in receptor-facilitated membrane localization of the enzyme. The beta gamma subunits of transducin were less effective at both enhancing the rate of receptor phosphorylation and binding to the COOH-terminus of beta ARK, suggesting that the enzyme preferentially binds specific beta gamma complexes. The beta gamma-mediated membrane localization of beta ARK serves to intimately link receptor activation to beta ARK-mediated desensitization.

Full Text

Duke Authors

Cited Authors

  • Pitcher, JA; Inglese, J; Higgins, JB; Arriza, JL; Casey, PJ; Kim, C; Benovic, JL; Kwatra, MM; Caron, MG; Lefkowitz, RJ

Published Date

  • August 28, 1992

Published In

Volume / Issue

  • 257 / 5074

Start / End Page

  • 1264 - 1267

PubMed ID

  • 1325672

Pubmed Central ID

  • 1325672

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1325672


  • eng

Conference Location

  • United States