Evidence map›Paper›PMID 30237420›Full record

ArticleNature communications2018

Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures.

Francesco Baschieri, Stéphane Dayot, Nadia Elkhatib, Nathalie Ly, Anahi Capmany, Kristine Schauer, Timo Betz, Danijela Matic Vignjevic, Renaud Poincloux, Guillaume Montagnac

Abstract read
In one paragraph

Article in Nature communications, 2018. 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
–field-weighted citation impact
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.

  1. Review
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  6. Exploring the interactions of integrins and CEACAM6 (Review).Experimental and therapeutic medicine · 2025
    Review
  7. Article
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  9. Review
  10. Article
  11. Polystyrene Microplastics Induce Photosynthetic Impairment inInternational journal of molecular sciences · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Emerging roles and mechanisms of ERK pathway mechanosensing.Cellular and molecular life sciences : CMLS · 2023
    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

10 authors.

Francesco BaschieriInserm U1170, Gustave Roussy Institute, Université Paris-Saclay, Villejuif, France. francesco.baschieri@gustaveroussy.fr.ORCID http://orcid.org/0000-0003-0218-5320
Stéphane DayotInserm U1170, Gustave Roussy Institute, Université Paris-Saclay, Villejuif, France.
Nadia ElkhatibInserm U1170, Gustave Roussy Institute, Université Paris-Saclay, Villejuif, France.
Nathalie LyInserm U1170, Gustave Roussy Institute, Université Paris-Saclay, Villejuif, France.
Anahi CapmanyInstitut Curie, CNRS UMR144, PSL Research University, Centre Universitaire, Paris, France.
Kristine SchauerInstitut Curie, CNRS UMR144, PSL Research University, Centre Universitaire, Paris, France.
Timo BetzInstitute of Cell Biology, Center of Molecular Biology of Inflammation, Cells-in-Motion Cluster of Excellence, University of Münster, Münster, Germany.
Danijela Matic VignjevicInstitut Curie, CNRS UMR144, PSL Research University, Centre Universitaire, Paris, France.ORCID http://orcid.org/0000-0003-4250-703X
Renaud PoinclouxInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID http://orcid.org/0000-0003-2884-1744
Guillaume MontagnacInserm U1170, Gustave Roussy Institute, Université Paris-Saclay, Villejuif, France. guillaume.montagnac@gustaveroussy.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility.

Indexed as

EndocytosisMechanotransduction, CellularCell LineCell ProliferationClathrin-Coated VesiclesHumansMAP Kinase Signaling SystemReceptors, Vitronectinintegrin alphaVbeta5Receptors, Vitronectin

Identifiers

PMID30237420
PMCPMC6148028

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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.