ArticleMolecular biology of the cell2017
Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
71 citing papers in PubMed, 117 citations in OpenAlex.
- Structural basis of active state coupling of metabotropic glutamate receptor 8 to beta-arrestins.Nature communications · 2026Article
- Factors modulating the assembly of human βNature structural & molecular biology · 2026Article
- Core conformation of arrestin coupling to parathyroid hormone type 1 receptor.Nature communications · 2026Article
- Membrane cholesterol modulates engagement of β-arrestin with the ghrelin receptor.Communications biology · 2026Article
- Distinct membrane binding properties of the two non-visual arrestins.Communications biology · 2026Article
- Structural Basis of GPCR-Biased Modulation.Handbook of experimental pharmacology · 2026Review
- A genetically encoded nanobody sensor reveals conformational diversity in β-arrestins orchestrated by distinct seven transmembrane receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of β-arrestin coupling to the metabotropic glutamate receptor mGlu3.Nature chemical biology · 2025Article
- An arginine switch drives the stepwise activation of β-arrestin by CXCR7.PLoS biology · 2025Article
- Helix-bundle and C-terminal GPCR domains differentially influence GRK-specific functions and β-arrestin-mediated regulation.Nature communications · 2025Article
- Lipids modulate the dynamics of GPCR:β-arrestin interaction.Nature communications · 2025Article
- How Ligands Achieve Biased Signaling toward Arrestins.Biochemistry · 2025Review
- Endosomal chemokine receptor signalosomes regulate central mechanisms underlying cell migration.eLife · 2025Article
- Receptor Determinants for β-Arrestin Functional Specificity atMolecular pharmacology · 2024Article
- Role of the V2R-βarrestin-Gβγ complex in promoting G protein translocation to endosomes.Communications biology · 2024Article
- Beneath the surface: endosomal GPCR signaling.Trends in biochemical sciences · 2024Review
- Structure, function and drug discovery of GPCR signaling.Molecular biomedicine · 2023Review
- Location bias: A "Hidden Variable" in GPCR pharmacology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- β-Arrestin-dependent and -independent endosomal G protein activation by the vasopressin type 2 receptor.eLife · 2023Article
- The NPXXY Motif Regulates β-Arrestin Recruitment by the CB1 Cannabinoid Receptor.Cannabis and cannabinoid research · 2023Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
G protein-coupled receptors (GPCRs) exhibit highly conserved activation and signaling mechanisms by which agonist stimulation leads to coupling of heterotrimeric G proteins and generation of second messenger response. This is followed by receptor phosphorylation, primarily in the carboxyl terminus but also in the cytoplasmic loops, and subsequent binding of arrestins. GPCRs typically recruit arrestins through two different sets of interactions, one involving phosphorylated receptor tail and the other mediated by the receptor core. The engagement of both set of interactions (tail and core) is generally believed to be necessary for arrestin-dependent functional outcomes such as receptor desensitization, endocytosis, and G protein-independent signaling. Here we demonstrate that a vasopressin receptor (V
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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.