Evidence map›Paper›PMID 28128308›Full record

ArticleNature communications2017

αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin.

Mitasha Bharadwaj, Nico Strohmeyer, Georgina P Colo, Jonne Helenius, Niko Beerenwinkel, Herbert B Schiller, Reinhard Fässler, Daniel J Müller

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Beyond MIDAS: AnACS omega · 2026
    Article
  5. Article
  6. Review
  7. Role and mechanism of Integrin α5β1 in bone formation and disease.Frontiers in cell and developmental biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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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

8 authors at 3 institutions in 2 countries.

Mitasha BharadwajEidgenössische Technische Hochschule (ETH) Zurich, Department of Biosystems Science and Engineering, 4058 Basel, Switzerland.
Nico StrohmeyerEidgenössische Technische Hochschule (ETH) Zurich, Department of Biosystems Science and Engineering, 4058 Basel, Switzerland.
Georgina P ColoMax Planck Institute of Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany.
Jonne HeleniusEidgenössische Technische Hochschule (ETH) Zurich, Department of Biosystems Science and Engineering, 4058 Basel, Switzerland.
Niko BeerenwinkelEidgenössische Technische Hochschule (ETH) Zurich, Department of Biosystems Science and Engineering, 4058 Basel, Switzerland.ORCID 0000-0002-0573-6119
Herbert B SchillerMax Planck Institute of Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany.ORCID 0000-0003-1914-3215
Reinhard FässlerMax Planck Institute of Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany.
Daniel J MüllerEidgenössische Technische Hochschule (ETH) Zurich, Department of Biosystems Science and Engineering, 4058 Basel, Switzerland.
Board of the Swiss Federal Institutes of Technology · CHMax Planck Institute of Biochemistry · DEHelmholtz Zentrum München · DE

Funding

European Research Council 322652
6 · The paper itself

Abstract

Upon binding to the extracellular matrix protein, fibronectin, αV-class and α5β1 integrins trigger the recruitment of large protein assemblies and strengthen cell adhesion. Both integrin classes have been functionally specified, however their specific roles in immediate phases of cell attachment remain uncharacterized. Here, we quantify the adhesion of αV-class and/or α5β1 integrins expressing fibroblasts initiating attachment to fibronectin (≤120 s) by single-cell force spectroscopy. Our data reveals that αV-class integrins outcompete α5β1 integrins. Once engaged, αV-class integrins signal to α5β1 integrins to establish additional adhesion sites to fibronectin, away from those formed by αV-class integrins. This crosstalk, which strengthens cell adhesion, induces α5β1 integrin clustering by RhoA/ROCK/myosin-II and Arp2/3-mediated signalling, whereas overall cell adhesion depends on formins. The dual role of both fibronectin-binding integrin classes commencing with an initial competition followed by a cooperative crosstalk appears to be a basic cellular mechanism in assembling focal adhesions to the extracellular matrix.

Indexed as

Actin-Related Protein 2-3 ComplexAnimalsCell AdhesionExtracellular MatrixFibroblastsFibronectinsFocal AdhesionsIntegrin alpha5beta1Integrin alphaVMiceMyosin Type IIProtein BindingrhoA GTP-Binding ProteinSignal TransductionSingle-Cell AnalysisSpectrum AnalysisActin-Related Protein 2-3 ComplexFibronectinsIntegrin alpha5beta1Integrin alphaVMyosin Type IIrhoA GTP-Binding Protein

Identifiers

PMID28128308
PMCPMC5290147
OpenAlexW2580231811

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.