Evidence map›Paper›PMID 27380548›Full record

ArticleACS nano2016

All Subdomains of the Talin Rod Are Mechanically Vulnerable and May Contribute To Cellular Mechanosensing.

Alexander William M Haining, Magdaléna von Essen, Simon J Attwood, Vesa P Hytönen, Armando Del Río Hernández

Abstract read
In one paragraph

Article in ACS nano, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

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  11. Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022
    Review
  12. Article
  13. Article
  14. Review
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  20. Talin folding as the tuning fork of cellular mechanotransduction.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

5 authors.

Alexander William M HainingCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London , London SW7 2AZ, United Kingdom.
Magdaléna von EssenBioMediTech, University of Tampere , Biokatu 6, FI-33520 Tampere, Finland.
Simon J AttwoodCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London , London SW7 2AZ, United Kingdom.
Vesa P HytönenBioMediTech, University of Tampere , Biokatu 6, FI-33520 Tampere, Finland.
Armando Del Río HernándezCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London , London SW7 2AZ, United Kingdom.

Funding

European Research Council 282051
6 · The paper itself

Abstract

Although the relevance of mechanotransduction in cell signaling is currently appreciated, the mechanisms that drive this process remain largely unknown. Mechanical unfolding of proteins may trigger distinct downstream signals in cells, providing a mechanism for cellular mechanotransduction. Force-induced unfolding of talin, a prominent focal adhesion protein, has been demonstrated previously for a small portion of its rod domain. Here, using single-molecule atomic force microscopy (smAFM), we show that the entire talin rod can be unfolded by mechanical extension, over a physiological range of forces between 10 and 40 pN. We also demonstrate, through a combination of smAFM and steered molecular dynamics, that the different bundles within the talin rod exhibit a distinct hierarchy of mechanical stability. These results provide a mechanism by which different force conditions within the cell control a graduated unfolding of the talin rod. Mechanical unfolding of the rod subdomains, and the subsequent effect on talin's binding interactions, would allow for a finely tuned cellular response to internally or externally applied forces.

Indexed as

Mechanotransduction, CellularProtein BindingTalinFocal AdhesionsMicroscopy, Atomic ForceTalinmechanobiologymechanotransductionprotein mechanostabilitysingle-molecule force spectroscopysteered molecular dynamics

Identifiers

PMID27380548
PMCPMC4982699

What OpenQuestion holds

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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.