The Adaptor Complex 2 Directly Interacts with the α1b-Adrenergic Receptor and Plays a Role in Receptor Endocytosis
Open Access
- 1 May 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (21) , 19331-19340
- https://doi.org/10.1074/jbc.m302110200
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Regulation of G Protein-Coupled Receptor Kinases and Arrestins During Receptor DesensitizationMolecular Pharmacology, 2003
- Differential Roles of Arrestin-2 Interaction with Clathrin and Adaptor Protein 2 in G Protein-coupled Receptor TraffickingJournal of Biological Chemistry, 2002
- Arresting developments in heptahelical receptor signaling and regulationTrends in Cell Biology, 2002
- β-Arrestin/AP-2 Interaction in G Protein-coupled Receptor InternalizationJournal of Biological Chemistry, 2002
- Adaptor-related proteinsCurrent Opinion in Cell Biology, 2001
- Clathrin coat construction in endocytosisCurrent Opinion in Structural Biology, 2000
- The β 2 -adrenergic receptor/βarrestin complex recruits the clathrin adaptor AP-2 during endocytosisProceedings of the National Academy of Sciences, 1999
- β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptorNature, 1996
- Epidermal Growth Factor Receptor Interaction with Clathrin Adaptors Is Mediated by the Tyr974-containing Internalization MotifJournal of Biological Chemistry, 1996
- Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosisCell, 1990