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.
Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors.
J. Pitcher,James Inglese,J. B. Higgins,J. Arriza,P. Casey,C. Kim,J. Benovic,M. Kwatra,M. Caron,R. Lefkowitz
Published 1992 in Science
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- Publication year
1992
- Venue
Science
- Publication date
1992-08-28
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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