1990/06/22 by Martin J. Lohse, Jeffrey Benovic, Juan Codina +2 · 3 citations
Biochemistry, Genetics and Molecular Biology · Medicine · Pharmacology, Toxicology and Pharmaceutics · #Receptor Mechanisms and Signaling #Renin-Angiotensin System Studies #Pharmacogenetics and Drug Metabolism
paper · doi:10.1126/science.2163110
openalex publication_date 1990/06/22 · openalex created_date 2016/06/24 · openalex updated_date 2026/08/01
Homologous or agonist-specific desensitization of beta-adrenergic receptors is thought to be mediated by a specific kinase, the beta-adrenergic receptor kinase (beta ARK). However, recent data suggest that a cofactor is required for this kinase to inhibit receptor function. The complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid protein homologous to the retinal protein arrestin. The protein, termed beta-arrestin, was expressed and partially purified. It inhibited the signaling function of beta ARK-phosphorylated beta-adrenergic receptors by more than 75 percent, but not that of rhodopsin. It is proposed that beta-arrestin in concert with beta ARK effects homologous desensitization of beta-adrenergic receptors.