Evidence map›Paper›PMID 26030356›Full record

ArticleScientific reports2015

Unraveling the molecular architecture of a G protein-coupled receptor/β-arrestin/Erk module complex.

Thomas Bourquard, Flavie Landomiel, Eric Reiter, Pascale Crépieux, David W Ritchie, Jérôme Azé, Anne Poupon

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. List2Net: Linking multiple lists of biological data in a network context.Computational and structural biotechnology journal · 2024
    Article
  4. Article
  5. Article
  6. The Two Non-Visual Arrestins Engage ERK2 Differently.Journal of molecular biology · 2022
    Article
  7. Scaffolding of Mitogen-Activated Protein Kinase Signaling by β-Arrestins.International journal of molecular sciences · 2022
    Review
  8. Constitutive signal bias mediated by the human GHRHR splice variant 1.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Many faces of the GPCR-arrestin interaction.Archives of pharmacal research · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

7 authors at 4 institutions in 1 country.

Thomas Bourquard1] BIOS group, INRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, F-37380 Nouzilly, France; CNRS, UMR7247, F-37380 Nouzilly, France; Université François Rabelais, 37041 Tours, France; IFCE, Nouzilly, F-37380 France [2] INRIA Nancy, 615 Rue du Jardin Botanique, Villers-lès-Nancy, 54600 France.
Flavie LandomielBIOS group, INRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, F-37380 Nouzilly, France; CNRS, UMR7247, F-37380 Nouzilly, France; Université François Rabelais, 37041 Tours, France; IFCE, Nouzilly, F-37380 France.
Eric ReiterBIOS group, INRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, F-37380 Nouzilly, France; CNRS, UMR7247, F-37380 Nouzilly, France; Université François Rabelais, 37041 Tours, France; IFCE, Nouzilly, F-37380 France.
Pascale CrépieuxBIOS group, INRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, F-37380 Nouzilly, France; CNRS, UMR7247, F-37380 Nouzilly, France; Université François Rabelais, 37041 Tours, France; IFCE, Nouzilly, F-37380 France.
David W RitchieINRIA Nancy, 615 Rue du Jardin Botanique, Villers-lès-Nancy, 54600 France.
Jérôme AzéBioinformatics group - AMIB INRIA - Laboratoire de Recherche en Informatique, Université Paris-Sud, Orsay, 91405 France.
Anne PouponBIOS group, INRA, UMR85, Unité Physiologie de la Reproduction et des Comportements, F-37380 Nouzilly, France; CNRS, UMR7247, F-37380 Nouzilly, France; Université François Rabelais, 37041 Tours, France; IFCE, Nouzilly, F-37380 France.
Physiologie de la Reproduction et des Comportements · FRCentre Inria de l'Université de Lorraine · FRCentre National de la Recherche Scientifique · FRInstitut national de recherche en informatique et en automatique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-arrestins serve as signaling scaffolds downstream of G protein-coupled receptors, and thus play a crucial role in a plethora of cellular processes. Although it is largely accepted that the ability of β-arrestins to interact simultaneously with many protein partners is key in G protein-independent signaling of GPCRs, only the precise knowledge of these multimeric arrangements will allow a full understanding of the dynamics of these interactions and their functional consequences. However, current experimental procedures for the determination of the three-dimensional structures of protein-protein complexes are not well adapted to analyze these short-lived, multi-component assemblies. We propose a model of the receptor/β-arrestin/Erk1 signaling module, which is consistent with most of the available experimental data. Moreover, for the β-arrestin/Raf1 and the β-arrestin/ERK interactions, we have used the model to design interfering peptides and shown that they compete with both partners, hereby demonstrating the validity of the predicted interaction regions.

Indexed as

Models, MolecularArrestinsbeta-ArrestinsExtracellular Signal-Regulated MAP KinasesHumansMAP Kinase Kinase 1Molecular Docking SimulationMultiprotein ComplexesProtein BindingProtein ConformationProto-Oncogene Proteins pp60(c-src)Receptors, G-Protein-CoupledSignal Transductionsrc Homology DomainsArrestinsbeta-ArrestinsExtracellular Signal-Regulated MAP KinasesMAP2K1 protein, humanMAP Kinase Kinase 1Multiprotein ComplexesProto-Oncogene Proteins pp60(c-src)Receptors, G-Protein-Coupled

Identifiers

PMID26030356
PMCPMC4649906
OpenAlexW1679394059

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.