Evidence map›Paper›PMID 26347956›Full record

ArticleNature communications2015

Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.

Fan Yang, Xiao Yu, Chuan Liu, Chang-Xiu Qu, Zheng Gong, Hong-Da Liu, Fa-Hui Li, Hong-Mei Wang, Dong-Fang He, Fan Yi and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 198 citations in OpenAlex.

  1. Review
  2. Review
  3. Factors modulating the assembly of human βNature structural & molecular biology · 2026
    Article
  4. Intrinsic conformational equilibria position arrestin-2 for activation.Protein science : a publication of the Protein Society · 2026
    Article
  5. Article
  6. GPCR Phospho-Barcodes and Biased Signaling.Handbook of experimental pharmacology · 2026
    Review
  7. Intrinsic conformational equilibria position arrestin-2 for activation.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Elucidating biased signaling in class A GPCRs.Trends in pharmacological sciences · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. The function of GPCRs in different bone cells.International journal of biological sciences · 2025
    Review
  16. Review
  17. Article
  18. Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024
    Review
  19. Beneath the surface: endosomal GPCR signaling.Trends in biochemical sciences · 2024
    Review
  20. Review

41 more citing papers are in PubMed but not listed here.

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

15 authors at 6 institutions in 3 countries.

Fan YangLaboratory of Quantum Biophysics and Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, 100101, China.
Xiao YuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Chuan LiuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Chang-Xiu QuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Zheng GongKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Hong-Da LiuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Fa-Hui LiLaboratory of Quantum Biophysics and Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, 100101, China.
Hong-Mei WangDepartment of Physiology, Shandong University School of Medicine, Jinan, Shandong 250012, China.
Dong-Fang HeKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Fan YiDepartment of Pharmacology, Shandong University School of Medicine, Jinan, Shandong 250012, China.
Chen SongDepartment of Biochemistry, University of Oxford, Oxford OX13QU, UK.
Chang-Lin TianHefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230027, China.
Kun-Hong XiaoDepartment of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
Jiang-Yun WangLaboratory of Quantum Biophysics and Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, 100101, China.
Jin-Peng SunKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University School of Medicine, 44 Wenhua Xi Road, Jinan, Shandong 250012, China.
Shandong University · CNChinese Academy of Sciences · CNInstitute of Biophysics · CNUniversity of Oxford · GBUniversity of Pittsburgh · USUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific arrestin conformations are coupled to distinct downstream effectors, which underlie the functions of many G-protein-coupled receptors (GPCRs). Here, using unnatural amino acid incorporation and fluorine-19 nuclear magnetic resonance ((19)F-NMR) spectroscopy, we demonstrate that distinct receptor phospho-barcodes are translated to specific β-arrestin-1 conformations and direct selective signalling. With its phosphate-binding concave surface, β-arrestin-1 'reads' the message in the receptor phospho-C-tails and distinct phospho-interaction patterns are revealed by (19)F-NMR. Whereas all functional phosphopeptides interact with a common phosphate binding site and induce the movements of finger and middle loops, different phospho-interaction patterns induce distinct structural states of β-arrestin-1 that are coupled to distinct arrestin functions. Only clathrin recognizes and stabilizes GRK2-specific β-arrestin-1 conformations. The identified receptor-phospho-selective mechanism for arrestin conformation and the spacing of the multiple phosphate-binding sites in the arrestin enable arrestin to recognize plethora phosphorylation states of numerous GPCRs, contributing to the functional diversity of receptors.

Indexed as

AnimalsArrestinsbeta-Arrestin 1beta-ArrestinsBinding SitesBlotting, WesternCattleClathrinEscherichia coliFluorineFluorine-19 Magnetic Resonance ImagingG-Protein-Coupled Receptor Kinase 2G-Protein-Coupled Receptor KinasesHEK293 CellsHumansMicroscopy, Confocal3,5-difluorotyrosineARRB1 protein, humanArrestinsbeta-Arrestin 1beta-ArrestinsClathrinFluorineG-Protein-Coupled Receptor Kinase 2G-protein-coupled receptor kinase 6G-Protein-Coupled Receptor KinasesGRK2 protein, humanPhosphate-Binding ProteinsPhosphoproteinsReceptors, G-Protein-CoupledTyrosine

Identifiers

PMID26347956
PMCPMC4569848
OpenAlexW2233128761

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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.