Evidence map›Paper›PMID 30028837›Full record

ArticlePLoS biology2018

Mechanotransduction in talin through the interaction of the R8 domain with DLC1.

Alexander William M Haining, Rolle Rahikainen, Ernesto Cortes, Dariusz Lachowski, Alistair Rice, Magdalena von Essen, Vesa P Hytönen, Armando Del Río Hernández

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 78 citations in OpenAlex.

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  8. The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  18. Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022
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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

8 authors at 2 institutions in 2 countries.

Alexander William M HainingCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London, London, United Kingdom.
Rolle RahikainenFaculty of Medicine and Life Sciences and BioMediTech, University of Tampere, Finland and Fimlab Laboratories, Tampere, Finland.
Ernesto CortesCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London, London, United Kingdom.
Dariusz LachowskiCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London, London, United Kingdom.
Alistair RiceCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London, London, United Kingdom.
Magdalena von EssenFaculty of Medicine and Life Sciences and BioMediTech, University of Tampere, Finland and Fimlab Laboratories, Tampere, Finland.
Vesa P HytönenFaculty of Medicine and Life Sciences and BioMediTech, University of Tampere, Finland and Fimlab Laboratories, Tampere, Finland.
Armando Del Río HernándezCellular and Molecular Biomechanics Laboratory, Department of Bioengineering, Imperial College London, London, United Kingdom.ORCID 0000-0001-5062-8910
Imperial College London · GBTampere University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanical unfolding of proteins is a cellular mechanism for force transduction with potentially broad implications in cell fate. Despite this, the mechanism by which protein unfolding elicits differential downstream signalling pathways remains poorly understood. Here, we used protein engineering, atomic force microscopy, and biophysical tools to delineate how protein unfolding controls cell mechanics. Deleted in liver cancer 1 (DLC1) is a negative regulator of Ras homolog family member A (RhoA) and cell contractility that regulates cell behaviour when localised to focal adhesions bound to folded talin. Using a talin mutant resistant to force-induced unfolding of R8 domain, we show that talin unfolding determines DLC1 downstream signalling and, consequently, cell mechanics. We propose that this new mechanism of mechanotransduction may have implications for a wide variety of associated cellular processes.

Indexed as

Mechanotransduction, CellularAnimalsCell MovementDisulfidesFocal AdhesionsGTPase-Activating ProteinsMiceMolecular Dynamics SimulationProtein BindingProtein DomainsProtein UnfoldingStructure-Activity RelationshipTalinTumor Suppressor ProteinsDisulfidesDLC-1 (deleted in liver cancer) protein, mouseGTPase-Activating ProteinsTalinTumor Suppressor Proteins

Identifiers

PMID30028837
PMCPMC6054372
OpenAlexW2883883757

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.