Evidence map›Paper›PMID 34887409›Full record

ArticleNature communications2021

Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR.

Yutaro Shiraishi, Yutaka Kofuku, Takumi Ueda, Shubhi Pandey, Hemlata Dwivedi-Agnihotri, Arun K Shukla, Ichio Shimada

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Intrinsic conformational equilibria position arrestin-2 for activation.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Intrinsic conformational equilibria position arrestin-2 for activation.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Arrestin recognizes GPCRs independently of the receptor state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Membrane mimetic-dependence of GPCR energy landscapes.Structure (London, England : 1993) · 2024
    Article
  10. Information Transmission in G Protein-Coupled Receptors.International journal of molecular sciences · 2024
    Review
  11. Article
  12. Article
  13. Membrane Mimetic-Dependence of GPCR Energy Landscapes.bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Yutaro ShiraishiLaboratory for Dynamic Structure of Biomolecules, RIKEN Center for Biosystems Dynamics Research (BDR), 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.ORCID 0000-0001-5502-1720
Yutaka KofukuGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.
Takumi UedaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID 0000-0001-9677-0912
Shubhi PandeyDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, 208016, India.
Hemlata Dwivedi-AgnihotriDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, 208016, India.
Arun K ShuklaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, 208016, India.ORCID 0000-0003-2910-8288
Ichio ShimadaLaboratory for Dynamic Structure of Biomolecules, RIKEN Center for Biosystems Dynamics Research (BDR), 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan. ichio.shimada@riken.jp.ORCID 0000-0001-5168-8894
Indian Institute of Technology Kanpur · INRIKEN Center for Biosystems Dynamics Research · JPThe University of Tokyo · JP

Funding

Wellcome Trust
6 · The paper itself

Abstract

β-arrestins (βarrs) play multifaceted roles in the function of G protein-coupled receptors (GPCRs). βarrs typically interact with phosphorylated C-terminal tail (C tail) and transmembrane core (TM core) of GPCRs. However, the effects of the C tail- and TM core-mediated interactions on the conformational activation of βarrs have remained elusive. Here, we show the conformational changes for βarr activation upon the C tail- and TM core-mediated interactions with a prototypical GPCR by nuclear magnetic resonance (NMR) spectroscopy. Our NMR analyses demonstrated that while the C tail-mediated interaction alone induces partial activation, in which βarr exists in equilibrium between basal and activated conformations, the TM core- and the C tail-mediated interactions together completely shift the equilibrium toward the activated conformation. The conformation-selective antibody, Fab30, promotes partially activated βarr into the activated-like conformation. This plasticity of βarr conformation in complex with GPCRs engaged in different binding modes may explain the multifunctionality of βarrs.

Indexed as

beta-Arrestin 1HumansMagnetic Resonance SpectroscopyProtein BindingProtein Conformation, beta-StrandProtein DomainsReceptors, G-Protein-Coupledbeta-Arrestin 1Receptors, G-Protein-Coupled

Identifiers

PMID34887409
PMCPMC8660791
OpenAlexW4200459747

What OpenQuestion holds

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Registered trials

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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.