c-Src Tyrosine Kinase Binds the β2-Adrenergic Receptor via Phospho-Tyr-350, Phosphorylates G-protein-linked Receptor Kinase 2, and Mediates Agonist-induced Receptor Desensitization
Open Access
- 1 April 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (16) , 13240-13247
- https://doi.org/10.1074/jbc.m011578200
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- β-Arrestin-Dependent Formation of β 2 Adrenergic Receptor-Src Protein Kinase ComplexesScience, 1999
- Physiological Regulation of G Protein-Linked SignalingPhysiological Reviews, 1999
- Src-mediated Tyrosine Phosphorylation of Dynamin Is Required for β2-Adrenergic Receptor Internalization and Mitogen-activated Protein Kinase SignalingPublished by Elsevier ,1999
- G Protein-coupled ReceptorsJournal of Biological Chemistry, 1998
- G-protein-coupled receptors: turn-ons and turn-offsCurrent Opinion in Neurobiology, 1998
- Role of Clathrin-mediated Endocytosis in Agonist-induced Down-regulation of the β2-Adrenergic ReceptorJournal of Biological Chemistry, 1998
- CELLULAR FUNCTIONS REGULATED BY SRC FAMILY KINASESAnnual Review of Cell and Developmental Biology, 1997
- β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptorNature, 1996
- The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity.Proceedings of the National Academy of Sciences, 1995
- Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein).Proceedings of the National Academy of Sciences, 1987