Feedback Regulation of β-Arrestin1 Function by Extracellular Signal-regulated Kinases
Open Access
- 1 June 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (23) , 15971-15974
- https://doi.org/10.1074/jbc.274.23.15971
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- β-Arrestins Regulate Mitogenic Signaling and Clathrin-mediated Endocytosis of the Insulin-like Growth Factor I ReceptorJournal of Biological Chemistry, 1998
- G Protein-coupled ReceptorsJournal of Biological Chemistry, 1998
- Insulin-like Growth Factor-I Receptor Internalization Regulates Signaling via the Shc/Mitogen-activated Protein Kinase Pathway, but Not the Insulin Receptor Substrate-1 PathwayJournal of Biological Chemistry, 1998
- Essential Role for G Protein-coupled Receptor Endocytosis in the Activation of Mitogen-activated Protein KinaseJournal of Biological Chemistry, 1998
- G Protein-coupled Receptors Mediate Two Functionally Distinct Pathways of Tyrosine Phosphorylation in Rat 1a FibroblastsPublished by Elsevier ,1997
- Clathrin-mediated Endocytosis of the β-Adrenergic Receptor Is Regulated by Phosphorylation/Dephosphorylation of β-Arrestin1Journal of Biological Chemistry, 1997
- An NGF-TrkA-Mediated Retrograde Signal to Transcription Factor CREB in Sympathetic NeuronsScience, 1997
- β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptorNature, 1996
- Role of β-Arrestin in Mediating Agonist-Promoted G Protein-Coupled Receptor InternalizationScience, 1996
- β-Arrestin: a Protein that Regulates β-adrenergic Receptor FunctionScience, 1990