ArticleThe Journal of biological chemistry2014
Mutation of three residues in the third intracellular loop of the dopamine D2 receptor creates an internalization-defective receptor.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- Molecular mechanism of β-arrestin 2 interaction with phosphorylated intracellular loop 3 of dopamine receptor D2.Communications biology · 2025Article
- An arginine switch drives the stepwise activation of β-arrestin by CXCR7.PLoS biology · 2025Article
- Comparison of the function of two novel human dopamine D2 receptor variants identifies a likely mechanism for their pathogenicity.Biochemical pharmacology · 2024Article
- G Protein-Coupled Receptor Kinase 2 Selectively Enhances β-Arrestin Recruitment to the DBiomolecules · 2023Article
- In-Cell Arrestin-Receptor Interaction Assays.Current protocols · 2023Article
- Novel Cannabinoid Receptor 2 (CB2) Low Lipophilicity Agonists Produce Distinct cAMP and Arrestin Signalling Kinetics without Bias.International journal of molecular sciences · 2023Article
- Investigating G-protein coupled receptor signalling with light-emitting biosensors.Frontiers in physiology · 2023Review
- Article
- Delineating the interactions between the cannabinoid CBBritish journal of pharmacology · 2022Article
- Signaling-Biased and Constitutively Active Dopamine D2 Receptor Variant.ACS chemical neuroscience · 2021Article
- A Gain-of-Function Variant in Dopamine D2 Receptor and Progressive Chorea and Dystonia Phenotype.Movement disorders : official journal of the Movement Disorder Society · 2021Article
- Arrestin recruitment to dopamine D2 receptor mediates locomotion but not incentive motivation.Molecular psychiatry · 2020Article
- Evaluating kratom alkaloids using PHASE.PloS one · 2020Article
- Extramembranous Regions in G Protein-Coupled Receptors: Cinderella in Receptor Biology?The Journal of membrane biology · 2019Review
- Cannabinoid CB1 and CB2 Receptor-Mediated Arrestin Translocation: Species, Subtype, and Agonist-Dependence.Frontiers in pharmacology · 2019Article
- Optical Control of Dopamine Receptors Using a Photoswitchable Tethered Inverse Agonist.Journal of the American Chemical Society · 2017Article
- Visualization of ligand-induced dopamine DScientific reports · 2017Article
- Desensitized D2 autoreceptors are resistant to trafficking.Scientific reports · 2017Article
- Dopamine: A Modulator of Circadian Rhythms in the Central Nervous System.Frontiers in cellular neuroscience · 2017Review
- Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Arrestins mediate desensitization and internalization of G protein-coupled receptors and also direct receptor signaling toward heterotrimeric G protein-independent signaling pathways. We previously identified a four-residue segment (residues 212-215) of the dopamine D2 receptor that is necessary for arrestin binding in an in vitro heterologous expression system but that also impairs receptor expression. We now describe the characterization of additional mutations at that arrestin binding site in the third intracellular loop. Mutating two (residues 214 and 215) or three (residues 213-215) of the four residues to alanine partially decreased agonist-induced recruitment of arrestin3 without altering activation of a G protein. Arrestin-dependent receptor internalization, which requires arrestin binding to β2-adaptin (the β2 subunit of the clathrin-associated adaptor protein AP2) and clathrin, was disproportionately affected by the three-residue mutation, with no agonist-induced internalization observed even in the presence of overexpressed arrestin or G protein-coupled receptor kinase 2. The disjunction between arrestin recruitment and internalization could not be explained by alterations in the time course of the receptor-arrestin interaction, the recruitment of G protein-coupled receptor kinase 2, or the receptor-induced interaction between arrestin and β2-adaptin, suggesting that the mutation impairs a property of the internalization complex that has not yet been identified.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.