Evidence map›Paper›PMID 26833789›Full record

ArticleThe Journal of cell biology2016

Modulation of FAK and Src adhesion signaling occurs independently of adhesion complex composition.

Edward R Horton, Jonathan D Humphries, Ben Stutchbury, Guillaume Jacquemet, Christoph Ballestrem, Simon T Barry, Martin J Humphries

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
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  4. Review
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  6. Review
  7. Review
  8. Review
  9. Focal adhesion kinase regulates tendon cell mechanoresponse and physiological tendon development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  10. Article
  11. Article
  12. Lineage Plasticity in SCLC Generates Non-Neuroendocrine Cells Primed for Vasculogenic Mimicry.Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. FAK in Cancer: From Mechanisms to Therapeutic Strategies.International journal of molecular sciences · 2022
    Review
  18. Article
  19. Article
  20. Article
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

7 authors at 3 institutions in 1 country.

Edward R HortonWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK.
Jonathan D HumphriesWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK.
Ben StutchburyWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK.
Guillaume JacquemetWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK.
Christoph BallestremWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK.
Simon T BarryOncology iMed, AstraZeneca, Cheshire SK10 4TG, England, UK.
Martin J HumphriesWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK martin.humphries@manchester.ac.uk.
Wellcome Centre for Cell-Matrix Research · GBUniversity of Manchester · GBAstraZeneca (United Kingdom) · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 092015Wellcome Trust 097820
6 · The paper itself

Abstract

Integrin adhesion complexes (IACs) form mechanochemical connections between the extracellular matrix and actin cytoskeleton and mediate phenotypic responses via posttranslational modifications. Here, we investigate the modularity and robustness of the IAC network to pharmacological perturbation of the key IAC signaling components focal adhesion kinase (FAK) and Src. FAK inhibition using AZ13256675 blocked FAK(Y397) phosphorylation but did not alter IAC composition, as reported by mass spectrometry. IAC composition was also insensitive to Src inhibition using AZD0530 alone or in combination with FAK inhibition. In contrast, kinase inhibition substantially reduced phosphorylation within IACs, cell migration and proliferation. Furthermore using fluorescence recovery after photobleaching, we found that FAK inhibition increased the exchange rate of a phosphotyrosine (pY) reporter (dSH2) at IACs. These data demonstrate that kinase-dependent signal propagation through IACs is independent of gross changes in IAC composition. Together, these findings demonstrate a general separation between the composition of IACs and their ability to relay pY-dependent signals.

Indexed as

Cell AdhesionFibroblastsFocal Adhesion Kinase 1Focal AdhesionsSignal Transductionsrc-Family KinasesAnimalsCell MovementCell ProliferationDose-Response Relationship, DrugHEK293 CellsHumansMiceNIH 3T3 CellsPhosphorylationPhosphotyrosineFocal Adhesion Kinase 1PhosphotyrosineProtein Kinase InhibitorsPTK2 protein, humansrc-Family Kinases

Identifiers

PMID26833789
PMCPMC4739608
OpenAlexW2274518044

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.