Agonist-dependent phosphorylation of the alpha 2-adrenergic receptor by the beta-adrenergic receptor kinase.

Détails

ID Serval
serval:BIB_19BDE6B4DA32
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Agonist-dependent phosphorylation of the alpha 2-adrenergic receptor by the beta-adrenergic receptor kinase.
Périodique
Journal of Biological Chemistry
Auteur(s)
Benovic J.L., Regan J.W., Matsui H., Mayor F., Cotecchia S., Leeb-Lundberg L.M., Caron M.G., Lefkowitz R.J.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
1987
Peer-reviewed
Oui
Volume
262
Numéro
36
Pages
17251-17253
Langue
anglais
Résumé
Desensitization of the beta-adrenergic receptor, a receptor which is coupled to the stimulation of adenylate cyclase, may be regulated via phosphorylation by a unique protein kinase. This recently discovered enzyme, known as the beta-adrenergic receptor kinase, only phosphorylates the agonist-occupied form of the beta-adrenergic receptor. To assess whether receptors coupled to the inhibition of adenylate cyclase might also be substrates, we examined the effects of beta-adrenergic receptor kinase on the partially purified human platelet alpha 2-adrenergic receptor. Phosphorylation of the reconstituted alpha 2-adrenergic receptor was dependent on agonist occupancy and was completely blocked by coincubation with alpha 2-antagonists. The time course of phosphorylation of the alpha 2-adrenergic receptor was virtually identical to that observed with the beta-adrenergic receptor with maximum stoichiometries of 7-8 mol of phosphate/mol of receptor in each case. In contrast, the alpha 1-adrenergic receptor, which is coupled to stimulation of phosphatidylinositol hydrolysis, is not a substrate for the beta-adrenergic receptor kinase. These results suggest that receptors coupled to either stimulation or inhibition of adenylate cyclase may be regulated by an agonist-dependent phosphorylation mediated by the beta-adrenergic receptor kinase.
Mots-clé
Affinity Labels/metabolism, Animals, Cricetinae, Phosphorylation, Photochemistry, Protein Kinases/metabolism, Receptors, Adrenergic, alpha/metabolism, Rhodopsin/metabolism, Time Factors
Pubmed
Web of science
Création de la notice
24/01/2008 11:05
Dernière modification de la notice
20/08/2019 12:50
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