Rapid Agonist-induced Desensitization and Internalization of the A2B Adenosine Receptor Is Mediated by a Serine Residue Close to the COOH Terminus
Open Access
- 1 August 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (32) , 30199-30207
- https://doi.org/10.1074/jbc.m010650200
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Arrestin Isoforms Dictate Differential Kinetics of A2B Adenosine Receptor TraffickingBiochemistry, 2000
- Shutoff and Agonist-Triggered Internalization of Protease-Activated Receptor 1 Can Be Separated by Mutation of Putative Phosphorylation Sites in the Cytoplasmic TailBiochemistry, 1999
- Dynamin-mediated Internalization of CaveolaeThe Journal of cell biology, 1998
- Modulation of the Arrestin-Clathrin Interaction in CellsJournal of Biological Chemistry, 1997
- Identification of an A2a Adenosine Receptor Domain Specifically Responsible for Mediating Short-Term DesensitizationBiochemistry, 1997
- The Role of Sequestration in G Protein-coupled Receptor ResensitizationJournal of Biological Chemistry, 1997
- β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptorNature, 1996
- Adenosine Receptor Subtypes: Characterization and Therapeutic RegulationAnnual Review of Pharmacology and Toxicology, 1995
- Epitope-tag vectors for eukaryotic protein productionGene, 1995
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976