Evidence map›Paper›PMID 41171905›Full record

ArticleScience advances2025

The mechanical response of vinculin.

Xuyao Liu, Jingzhun Liu, Yinan Wang, Mingxi Yao, Karen B Baker, Benjamin Klapholz, Nicholas H Brown, Benjamin T Goult, Jie Yan

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. [Mechanobiology of peripheral nerve development: mechanical properties, sensing, and response].Zhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery · 2026
    Review
  2. Podosomes and Mechanical Force.Results and problems in cell differentiation · 2026
    Review
  3. Review
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

9 authors.

Xuyao LiuDepartment of Physics, National University of Singapore, Singapore 117542, Singapore.
Jingzhun LiuDepartment of Physics, National University of Singapore, Singapore 117542, Singapore.ORCID 0000-0003-4585-8310
Yinan WangDepartment of Physics, National University of Singapore, Singapore 117542, Singapore.
Mingxi YaoDepartment of Biomedical Engineering, Southern University of Science and Technology, Shenzhen 518055, P. R. China.ORCID 0000-0002-3905-8475
Karen B BakerSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, UK.ORCID 0000-0001-7628-1978
Benjamin KlapholzDepartment of Physiology, Development, and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 1DY, UK.ORCID 0000-0002-3681-4415
Nicholas H BrownDepartment of Physiology, Development, and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 1DY, UK.ORCID 0000-0002-8958-7017
Benjamin T GoultSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, UK.ORCID 0000-0002-3438-2807
Jie YanDepartment of Physics, National University of Singapore, Singapore 117542, Singapore.ORCID 0000-0002-8555-7291

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vinculin is a mechanosensitive adaptor that links actin to cell-matrix and cell-cell adhesions. Known as a mechanoeffector, it is recruited to adhesion sites under force via mechanotransducers talin and α-catenin. Here, we examine vinculin's mechanical properties to assess its role as a mechanotransducer. We find that at physiological loading rates, vinculin domains unfold at forces of 5 to 15 pN and refold rapidly when forces drop to 1 pN. This behavior is reminiscent of force-dependent switches in talin and α-catenin, suggesting vinculin domains also function as molecular switches. Unfolding induces large extension changes up to 150 nm in steps of 20 to 30 nm. These findings reveal that vinculin exhibits a previously unrecognized mechanical response, with dynamic folding/unfolding under force acting as a buffering mechanism. Given its role as a scaffold for many proteins, this mechanosensitive behavior supports a model where vinculin functions directly as a mechanotransducer, recruiting binding partners in a force-dependent manner.

Indexed as

Mechanotransduction, CellularVinculinalpha CateninAnimalsBiomechanical PhenomenaHumansProtein BindingProtein DomainsProtein FoldingProtein UnfoldingTalinalpha CateninTalinVinculin

Identifiers

PMID41171905
PMCPMC12577685

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.