Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors.
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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Related Subject Headings
- beta-Adrenergic Receptor Kinases
- Virulence Factors, Bordetella
- Time Factors
- Rhodopsin
- Recombinant Fusion Proteins
- Receptors, Adrenergic, beta
- Protein Processing, Post-Translational
- Protein Kinases
- Phosphorylation
- Molecular Sequence Data
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- beta-Adrenergic Receptor Kinases
- Virulence Factors, Bordetella
- Time Factors
- Rhodopsin
- Recombinant Fusion Proteins
- Receptors, Adrenergic, beta
- Protein Processing, Post-Translational
- Protein Kinases
- Phosphorylation
- Molecular Sequence Data