Evidence map›Paper›PMID 28302906›Full record

ArticleJournal of cell science2017

Distinct focal adhesion protein modules control different aspects of mechanotransduction.

Ben Stutchbury, Paul Atherton, Ricky Tsang, De-Yao Wang, Christoph Ballestrem

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
8.4field-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

101 citing papers in PubMed, 193 citations in OpenAlex.

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41 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Ben StutchburyWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, England, UK.ORCID 0000-0002-4231-9314
Paul AthertonWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, England, UK.ORCID 0000-0003-3098-674X
Ricky TsangWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, England, UK.ORCID 0000-0003-0274-9827
De-Yao WangWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, England, UK.ORCID 0000-0001-6431-4680
Christoph BallestremWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, England, UK christoph.ballestrem@manchester.ac.uk.ORCID 0000-0002-5375-7985
Wellcome Centre for Cell-Matrix Research · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J012254/1Biotechnology and Biological Sciences Research Council BB/P000681/1Wellcome TrustWellcome Trust 088785/Z/09/ZWellcome Trust 099734/Z/12/Z
6 · The paper itself

Abstract

Focal adhesions (FAs) are macromolecular complexes that regulate cell adhesion and mechanotransduction. By performing fluorescence recovery after photobleaching (FRAP) and fluorescence loss after photoactivation (FLAP) experiments, we found that the mobility of core FA proteins correlates with their function. Structural proteins such as tensin, talin and vinculin are significantly less mobile in FAs than signaling proteins such as FAK (also known as PTK2) and paxillin. The mobilities of the structural proteins are directly influenced by substrate stiffness, suggesting that they are involved in sensing the rigidity of the extracellular environment. The turnover rates of FAK and paxillin, as well as kindlin2 (also known as FERMT2), are not influenced by substrate stiffness. By using specific Src and FAK inhibitors, we reveal that force-sensing by vinculin occurs independently of FAK and paxillin phosphorylation. However, their phosphorylation is required for downstream Rac1-driven cellular processes, such as protrusion and cell migration. Overall, we show that the FA is composed of different functional modules that separately control mechanosensing and the cellular mechano-response.

Indexed as

Mechanotransduction, CellularAnimalsCell MovementExtracellular MatrixFluorescence Recovery After PhotobleachingFocal Adhesion Protein-Tyrosine KinasesFocal AdhesionsMiceModels, BiologicalNIH 3T3 CellsPaxillinPhosphorylationPhosphotyrosineProtein TransportPseudopodiaSignal TransductionFocal Adhesion Protein-Tyrosine KinasesPaxillinPhosphotyrosinesrc-Family KinasesVinculinFAKFocal adhesionMechanotransductionPaxillinTalinVinculin

Identifiers

PMID28302906
PMCPMC5450230
OpenAlexW2594954404

What OpenQuestion holds

Textmetadata
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.