Evidence map›Paper›PMID 33335089›Full record

ArticleNature communications2020

Metavinculin modulates force transduction in cell adhesion sites.

Verena Kanoldt, Carleen Kluger, Christiane Barz, Anna-Lena Schweizer, Deepak Ramanujam, Lukas Windgasse, Stefan Engelhardt, Anna Chrostek-Grashoff, Carsten Grashoff

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
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  5. The mechanical response of vinculin.Science advances · 2025
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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

9 authors at 3 institutions in 2 countries.

Verena KanoldtDepartment of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, 48149, Münster, Germany.
Carleen KlugerMax Planck Institute of Biochemistry, Group of Molecular Mechanotransduction, 82152, Martinsried, Germany.
Christiane BarzMax Planck Institute of Biochemistry, Group of Molecular Mechanotransduction, 82152, Martinsried, Germany.
Anna-Lena SchweizerDepartment of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, 48149, Münster, Germany.ORCID 0000-0003-1836-9108
Deepak RamanujamInstitute of Pharmacology and Toxicology, Technical University of Munich, 80802, Munich, Germany.
Lukas WindgasseDepartment of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, 48149, Münster, Germany.
Stefan EngelhardtInstitute of Pharmacology and Toxicology, Technical University of Munich, 80802, Munich, Germany.ORCID 0000-0001-5378-8661
Anna Chrostek-GrashoffDepartment of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, 48149, Münster, Germany.
Carsten GrashoffDepartment of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, 48149, Münster, Germany. grashoff@wwu.de.ORCID 0000-0003-0118-9231
University of Münster · DEMax Planck Institute of Biochemistry · DEGerman Centre for Cardiovascular Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vinculin is a ubiquitously expressed protein, crucial for the regulation of force transduction in cells. Muscle cells express a vinculin splice-isoform called metavinculin, which has been associated with cardiomyopathies. However, the molecular function of metavinculin has remained unclear and its role for heart muscle disorders undefined. Here, we have employed a set of piconewton-sensitive tension sensors to probe metavinculin mechanics in cells. Our experiments reveal that metavinculin bears higher molecular forces but is less frequently engaged as compared to vinculin, leading to altered force propagation in cell adhesions. In addition, we have generated knockout mice to investigate the consequences of metavinculin loss in vivo. Unexpectedly, these animals display an unaltered tissue response in a cardiac hypertrophy model. Together, the data reveal that the transduction of cell adhesion forces is modulated by expression of metavinculin, yet its role for heart muscle function seems more subtle than previously thought.

Indexed as

AnimalsCell AdhesionFibroblastsFluorescence Recovery After PhotobleachingFocal AdhesionsGene ExpressionHEK293 CellsHumansIntegrinsIntercellular JunctionsMiceMice, KnockoutMyocardiumProtein IsoformsSignal TransductionTalinIntegrinsmetavinculinProtein IsoformsTalinTln1 protein, mouseVCL protein, humanVcl protein, mouseVinculin

Identifiers

PMID33335089
PMCPMC7747745
OpenAlexW3112461481

What OpenQuestion holds

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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.