Evidence map›Paper›PMID 33141174›Full record

ArticleThe Journal of cell biology2020

αv-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation.

María Benito-Jardón, Nico Strohmeyer, Sheila Ortega-Sanchís, Mitasha Bharadwaj, Markus Moser, Daniel J Müller, Reinhard Fässler, Mercedes Costell

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-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

26 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
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  7. Review
  8. Compressed Cells Facilitate Adhesion Through Glycocalyx.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  9. Article
  10. Fibronectin matrix assembly at a glance.Journal of cell science · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Shaping Oncogenic Microenvironments: Contribution of Fibronectin.Frontiers in cell and developmental biology · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

María Benito-JardónDepartment of Biochemistry and Molecular Biology, Universitat de València, Burjassot, Spain.
Nico StrohmeyerEidgenössische Technische Hochschule Zürich, Basel, Switzerland.
Sheila Ortega-SanchísDepartment of Biochemistry and Molecular Biology, Universitat de València, Burjassot, Spain.
Mitasha BharadwajEidgenössische Technische Hochschule Zürich, Basel, Switzerland.
Markus MoserMax Planck Institute of Biochemistry, Martinsried, Germany.
Daniel J MüllerEidgenössische Technische Hochschule Zürich, Basel, Switzerland.
Reinhard FässlerMax Planck Institute of Biochemistry, Martinsried, Germany.
Mercedes CostellDepartment of Biochemistry and Molecular Biology, Universitat de València, Burjassot, Spain.
Board of the Swiss Federal Institutes of Technology · CHUniversitat de València · ESMax Planck Institute of Biochemistry · DE

Funding

European Research Council 810104
6 · The paper itself

Abstract

Fibronectin (FN) is an essential glycoprotein of the extracellular matrix; binds integrins, syndecans, collagens, and growth factors; and is assembled by cells into complex fibrillar networks. The RGD motif in FN facilitates cell binding- and fibrillogenesis through binding to α5β1 and αv-class integrins. However, whether RGD is the sole binding site for αv-class integrins is unclear. Most notably, substituting aspartate with glutamate (RGE) was shown to eliminate integrin binding in vitro, while mouse genetics revealed that FNRGE preserves αv-class integrin binding and fibrillogenesis. To address this conflict, we employed single-cell force spectroscopy, engineered cells, and RGD motif-deficient mice (Fn1ΔRGD/ΔRGD) to search for additional αv-class integrin-binding sites. Our results demonstrate that α5β1 and αv-class integrins solely recognize the FN-RGD motif and that αv-class, but not α5β1, integrins retain FN-RGE binding. Furthermore, Fn1ΔRGD/ΔRGD tissues and cells assemble abnormal and dysfunctional FNΔRGD fibrils in a syndecan-dependent manner. Our data highlight the central role of FN-RGD and the functionality of FN-RGE for αv-class integrins.

Indexed as

MutationAnimalsMiceMice, Mutant StrainsOligopeptidesReceptors, Vitronectinarginyl-glycyl-aspartic acidarginyl-glycyl-glutamic acidintegrin alphavbeta1OligopeptidesReceptors, Vitronectin

Identifiers

PMID33141174
PMCPMC7644020
OpenAlexW3097564287

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.