Direct binding of β‐arrestins to two distinct intracellular domains of the δ opioid receptor
Open Access
- 15 March 2001
- journal article
- Published by Wiley in Journal of Neurochemistry
- Vol. 76 (6) , 1887-1894
- https://doi.org/10.1046/j.1471-4159.2001.00204.x
Abstract
β‐Arrestins regulate opioid receptor‐mediated signal transduction and play an important role in opiate‐induced analgesia and tolerance/dependence. This study was carried out to measure the direct interaction between β‐arrestins and opioid receptor. Immunoprecipitation experiments demonstrated that β‐arrestin 1 physically interacts with delta opioid receptor (DOR) co‐expressed in human embryonic kidney 293 cells in an agonist‐enhanced manner and truncation of the carboxyl terminus of DOR partially impairs the interaction. In vitro data from glutathione‐S‐transferase pull‐down assay showed that the carboxyl terminus (CT) and the third intracellular loop (I3L) of DOR are both capable of and either domain is sufficient for binding to β‐arrestin 1 and 2. Surface plasmon resonance determination further revealed that binding of CT and I3L of DOR to β‐arrestin is additive, suggesting these two domains bind at distinctly different sites on β‐arrestin without considerable spatial hindrance. This study demonstrated for the first time the direct binding of β‐arrestins to the two distinct domains, the carboxyl terminus and the third intracellular loop, of DOR.Keywords
This publication has 37 references indexed in Scilit:
- Anti-HIV Agent Trichosanthin Enhances the Capabilities of Chemokines to Stimulate Chemotaxis and G Protein Activation, and This Is Mediated through Interaction of Trichosanthin and Chemokine ReceptorsThe Journal of Experimental Medicine, 1999
- A Conserved Arginine in the Distal Third Intracellular Loop of the μ‐Opioid Receptor Is Required for G Protein ActivationJournal of Neurochemistry, 1999
- Selective Interference of β-Arrestin 1 with κ and δ but Not μ Opioid Receptor/G Protein CouplingJournal of Biological Chemistry, 1998
- δ and κ Opioid Receptors Are Differentially Regulated by Dynamin-dependent Endocytosis When Activated by the Same Alkaloid AgonistJournal of Biological Chemistry, 1997
- μ and δ Opioid Receptors Are Differentially Desensitized by the Coexpression of β-Adrenergic Receptor Kinase 2 and β-Arrestin 2 in Xenopus OocytesPublished by Elsevier ,1997
- Carboxyl Terminus of Delta Opioid Receptor Is Required for Agonist-Dependent Receptor PhosphorylationBiochemical and Biophysical Research Communications, 1997
- Synergistic Regulation of m2 Muscarinic Acetylcholine Receptor Desensitization and Sequestration by G Protein-coupled Receptor Kinase-2 and β-Arrestin-1Journal of Biological Chemistry, 1997
- Interaction of Arrestins with Intracellular Domains of Muscarinic and α2-Adrenergic ReceptorsPublished by Elsevier ,1997
- X‐Arrestin: a new retinal arrestin mapping to the X chromosomeFEBS Letters, 1993
- Rhodopsin Phosphorylation by Transiently Expressed Human βArak1: A new Method for Drug DevelopmentJournal of Receptor Research, 1993