Evidence map›Paper›PMID 30462575›Full record

ArticleMolecular biology of the cell2019

Cellular tension encodes local Src-dependent differential β

Richard De Mets, Irene Wang, Martial Balland, Christiane Oddou, Philippe Moreau, Bertrand Fourcade, Corinne Albiges-Rizo, Antoine Delon, Olivier Destaing

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. 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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. New perspectives on integrin-dependent adhesions.Current opinion in cell biology · 2020
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Richard De MetsLaboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
Irene WangLaboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
Martial BallandLaboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
Christiane OddouInstitut Albert Bonniot, Université Joseph Fourier, INSERM U823, CNRS ERL 5284, Grenoble Alpessite Santé, F38042 Grenoble Cedex 09, France.
Philippe MoreauLaboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
Bertrand FourcadeLaboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
Corinne Albiges-RizoInstitut Albert Bonniot, Université Joseph Fourier, INSERM U823, CNRS ERL 5284, Grenoble Alpessite Santé, F38042 Grenoble Cedex 09, France.
Antoine DelonLaboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
Olivier DestaingInstitut Albert Bonniot, Université Joseph Fourier, INSERM U823, CNRS ERL 5284, Grenoble Alpessite Santé, F38042 Grenoble Cedex 09, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrins are transmembrane receptors that have a pivotal role in mechanotransduction processes by connecting the extracellular matrix to the cytoskeleton. Although it is well established that integrin activation/inhibition cycles are due to highly dynamic interactions, whether integrin mobility depends on local tension and cytoskeletal organization remains surprisingly unclear. Using an original approach combining micropatterning on glass substrates to induce standardized local mechanical constraints within a single cell with temporal image correlation spectroscopy, we measured the mechanosensitive response of integrin mobility at the whole cell level and in adhesion sites under different mechanical constraints. Contrary to β1 integrins, high tension increases β3 integrin residence time in adhesive regions. Chimeric integrins and structure-function studies revealed that the ability of β3 integrins to specifically sense local tensional organization is mostly encoded by its cytoplasmic domain and is regulated by tuning the affinity of its NPXY domains through phosphorylation by Src family kinases.

Indexed as

AnimalsBiomechanical PhenomenaCell AdhesionFibroblastsGreen Fluorescent ProteinsIntegrin beta1Integrin beta3Mechanotransduction, CellularMiceModels, BiologicalPhosphorylationProtein DomainsProtein TransportSpectrum Analysissrc-Family KinasesGreen Fluorescent ProteinsIntegrin beta1Integrin beta3src-Family Kinases

Identifiers

PMID30462575
PMCPMC6589565
OpenAlexW2900872496

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.