Evidence map›Paper›PMID 32978252›Full record

ArticleThe Journal of biological chemistry2020

Allosteric activation of proto-oncogene kinase Src by GPCR-beta-arrestin complexes.

Natalia Pakharukova, Ali Masoudi, Biswaranjan Pani, Dean P Staus, Robert J Lefkowitz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
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  13. Article
  14. β-arrestins Are Scaffolding Proteins Required for Shh-Mediated Axon Guidance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  15. Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024
    Review
  16. Review
  17. Article
  18. Signal transduction at GPCRs: Allosteric activation of the ERK MAPK by β-arrestin.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Pharmacological reviews · 2023
    Review
  20. Review
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

5 authors at 2 institutions in 1 country.

Natalia PakharukovaDepartment of Medicine, Duke University Medical Center, Durham, North Carolina, USA.
Ali MasoudiDepartment of Medicine, Duke University Medical Center, Durham, North Carolina, USA.
Biswaranjan PaniDepartment of Medicine, Duke University Medical Center, Durham, North Carolina, USA.
Dean P StausDepartment of Medicine, Duke University Medical Center, Durham, North Carolina, USA.
Robert J LefkowitzDepartment of Medicine, Duke University Medical Center, Durham, North Carolina, USA; Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA; Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina, USA. Electronic address: lefko001@receptor-biol.duke.edu.
Duke Medical Center · USHoward Hughes Medical Institute · US

Funding

Molecular Regulation of Cardiovascular 7 TM ReceptorsR01HL016037 · NHLBI · DUKE UNIVERSITY · PI ROBERT J LEFKOWITZ · 1985 to 2026
$14.5M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL016037
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) initiate signaling cascades via G-proteins and beta-arrestins (βarr). βarr-dependent actions begin with recruitment of βarr to the phosphorylated receptor tail and are followed by engagement with the receptor core. βarrs are known to act as adaptor proteins binding receptors and various effectors, but it is unclear whether in addition to the scaffolding role βarrs can allosterically activate their downstream targets. Here we demonstrate the direct allosteric activation of proto-oncogene kinase Src by GPCR-βarr complexes

Indexed as

Allosteric Regulationbeta-Arrestin 1Enzyme ActivationHumansKineticsMutagenesis, Site-DirectedNanostructuresPeptidesPhosphorylationProtein BindingProto-Oncogene MasReceptor, Muscarinic M2Receptors, Adrenergic, beta-2Receptors, VasopressinRecombinant Proteinssrc-Family Kinasesbeta-Arrestin 1MAS1 protein, humanPeptidesProto-Oncogene MasReceptor, Muscarinic M2Receptors, Adrenergic, beta-2Receptors, VasopressinRecombinant Proteinssrc-Family Kinasesallosteric regulationarrestinGPCRG protein-coupled receptorssignal transductionSrc

Identifiers

PMID32978252
PMCPMC7864071
OpenAlexW3088719539

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.