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Publication Detail
Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Pitcher JA, Inglese J, Higgins JB, Arriza JL, Casey PJ, Kim C, Benovic JL, Kwatra MM, Caron MG, Lefkowitz RJ
  • Publication date:
  • Pagination:
    1264, 1267
  • Journal:
  • Volume:
  • Issue:
  • Country:
  • Print ISSN:
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  • Keywords:
    Amino Acid Sequence, Animals, Cattle, Cyclic AMP-Dependent Protein Kinases, Dose-Response Relationship, Drug, Escherichia coli, GTP-Binding Proteins, Gene Expression Regulation, In Vitro Techniques, Molecular Sequence Data, Phosphorylation, Protein Kinases, Protein Processing, Post-Translational, Receptors, Adrenergic, beta, Recombinant Fusion Proteins, Rhodopsin, Time Factors, Virulence Factors, Bordetella, beta-Adrenergic Receptor Kinases
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.
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