beta-Arrestin: a protein that regulates beta-adrenergic receptor function
- PMID: 2163110
- DOI: 10.1126/science.2163110
beta-Arrestin: a protein that regulates beta-adrenergic receptor function
Abstract
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.
Similar articles
-
Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems.J Biol Chem. 1992 Apr 25;267(12):8558-64. J Biol Chem. 1992. PMID: 1349018
-
Overexpression of beta-arrestin and beta-adrenergic receptor kinase augment desensitization of beta 2-adrenergic receptors.J Biol Chem. 1993 Feb 15;268(5):3201-8. J Biol Chem. 1993. PMID: 8381421
-
Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.J Biol Chem. 1992 Sep 5;267(25):17882-90. J Biol Chem. 1992. PMID: 1517224
-
G-protein-coupled receptor kinases.Trends Biochem Sci. 1991 Oct;16(10):387-91. doi: 10.1016/0968-0004(91)90157-q. Trends Biochem Sci. 1991. PMID: 1664548 Review.
-
G-protein-coupled receptors: regulatory role of receptor kinases and arrestin proteins.Cold Spring Harb Symp Quant Biol. 1992;57:127-33. doi: 10.1101/sqb.1992.057.01.016. Cold Spring Harb Symp Quant Biol. 1992. PMID: 1339651 Review. No abstract available.
Cited by
-
Molecular mechanism of β-arrestin-2 pre-activation by phosphatidylinositol 4,5-bisphosphate.EMBO Rep. 2024 Oct;25(10):4190-4205. doi: 10.1038/s44319-024-00239-x. Epub 2024 Sep 6. EMBO Rep. 2024. PMID: 39242774 Free PMC article.
-
Beta-arrestin 1 mediated Src activation via Src SH3 domain revealed by cryo-electron microscopy.bioRxiv [Preprint]. 2024 Aug 6:2024.07.31.605623. doi: 10.1101/2024.07.31.605623. bioRxiv. 2024. PMID: 39131402 Free PMC article. Preprint.
-
Role of the V2R-βarrestin-Gβγ complex in promoting G protein translocation to endosomes.Commun Biol. 2024 Jul 7;7(1):826. doi: 10.1038/s42003-024-06512-y. Commun Biol. 2024. PMID: 38972875 Free PMC article.
-
G Protein-Coupled Receptors: A Century of Research and Discovery.Circ Res. 2024 Jun 21;135(1):174-197. doi: 10.1161/CIRCRESAHA.124.323067. Epub 2024 Jun 20. Circ Res. 2024. PMID: 38900852 Review.
-
Arrestins: A Small Family of Multi-Functional Proteins.Int J Mol Sci. 2024 Jun 6;25(11):6284. doi: 10.3390/ijms25116284. Int J Mol Sci. 2024. PMID: 38892473 Free PMC article. Review.
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
