ArticleCell reports2019
Conformational Sensors and Domain Swapping Reveal Structural and Functional Differences between β-Arrestin Isoforms.
Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 65 citations in OpenAlex.
- Configurational diversity of metabotropic glutamate receptor complexes with beta-arrestins.Nature communications · 2026Article
- Membrane-domain compartmentalization of active GPCRs by β-arrestins through PtdIns(4,5)PNature chemical biology · 2025Article
- 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
- Article
- Structure-guided engineering of biased-agonism in the human niacin receptor via single amino acid substitution.Nature communications · 2024Article
- Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors.Science (New York, N.Y.) · 2024Article
- Association of Neurokinin-1 Receptor Signaling Pathways with Cancer.Current medicinal chemistry · 2024Review
- Enabling technology and core theory of synthetic biology.Science China. Life sciences · 2023Review
- Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation.Molecular cell · 2023Article
- Article
- A community Biased Signaling Atlas.Nature chemical biology · 2023Article
- Comparative Study of Elabela and Apelin on Apelin Receptor Activation Through β-Arrestin Recruitment.Molecular biotechnology · 2023Article
- β-arrestin1 and 2 exhibit distinct phosphorylation-dependent conformations when coupling to the same GPCR in living cells.Nature communications · 2022Article
- G protein-coupled receptor signaling: transducers and effectors.American journal of physiology. Cell physiology · 2022Review
- Allosteric modulation of GPCR-induced β-arrestin trafficking and signaling by a synthetic intrabody.Nature communications · 2022Article
- Emerging structural insights into GPCR-β-arrestin interaction and functional outcomes.Current opinion in structural biology · 2022Review
- Community guidelines for GPCR ligand bias: IUPHAR review 32.British journal of pharmacology · 2022Review
- Making the switch: The role of Gq in driving GRK selectivity at GPCRs.Science signaling · 2022Article
- Comparative Immunogenicity of Bacterially Expressed Soluble Trimers and Nanoparticle Displayed Influenza Hemagglutinin Stem Immunogens.Frontiers in immunology · 2022Article
- Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR.Nature communications · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
19 authors at 8 institutions in 5 countries.
Funding
Abstract
Desensitization, signaling, and trafficking of G-protein-coupled receptors (GPCRs) are critically regulated by multifunctional adaptor proteins, β-arrestins (βarrs). The two isoforms of βarrs (βarr1 and 2) share a high degree of sequence and structural similarity; still, however, they often mediate distinct functional outcomes in the context of GPCR signaling and regulation. A mechanistic basis for such a functional divergence of βarr isoforms is still lacking. By using a set of complementary approaches, including antibody-fragment-based conformational sensors, we discover structural differences between βarr1 and 2 upon their interaction with activated and phosphorylated receptors. Interestingly, domain-swapped chimeras of βarrs display robust complementation in functional assays, thereby linking the structural differences between receptor-bound βarr1 and 2 with their divergent functional outcomes. Our findings reveal important insights into the ability of βarr isoforms to drive distinct functional outcomes and underscore the importance of integrating this aspect in the current framework of biased agonism.
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What OpenQuestion holds
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.