Evidence map›Paper›PMID 41269158›Full record

ArticleThe Journal of cell biology2026

Talin-tensin3 interactions regulate fibrillar adhesion formation and tensin3 phase separation.

Xingchen Li, Rafaella Konstantinou, Vinod Kumar Meena, Saba Notash, Komal Khalil, Tom Whalley, Paul Atherton, Igor Barsukov, Thomas Zacharchenko, Christoph Ballestrem

Abstract read
In one paragraph

Article in The Journal of cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

10 authors.

Xingchen LiFaculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0000-0003-2027-3770
Rafaella KonstantinouFaculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0000-0003-0017-7300
Vinod Kumar MeenaFaculty of Health and Life Sciences, Institute of Systems, Molecular and Integrative Biology, University of Liverpool , Liverpool, UK.ORCID 0000-0002-1175-5631
Saba NotashFaculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0009-0005-8691-2901
Komal KhalilFaculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0000-0001-9809-417X
Tom WhalleyFaculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0009-0002-6852-9560
Paul AthertonFaculty of Health and Life Sciences, Institute of Systems, Molecular and Integrative Biology, University of Liverpool , Liverpool, UK.ORCID 0000-0003-3098-674X
Igor Barsukov *Faculty of Health and Life Sciences, Institute of Systems, Molecular and Integrative Biology, University of Liverpool , Liverpool, UK.ORCID 0000-0003-4406-9803
Thomas Zacharchenko *Faculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0000-0001-5621-8605
Christoph Ballestrem *Faculty of Biology, Medicine and Health, Wellcome Centre for Cell-Matrix Research, University of Manchester , Manchester, UK.ORCID 0000-0002-5375-7985

Funding

Biotechnology and Biological Sciences Research Council BB/V016326/1Biotechnology and Biological Sciences Research Council BB/Y004841/1Biotechnology and Biological Sciences Research Council BB/Y005414/1Engineering and Physical Sciences Research Council EP/S022201/1Royal Society RG/R1/241366University of ManchesterWellcome TrustWellcome Trust 203128/A/16/Z
6 · The paper itself

Abstract

Integrin-mediated cell-matrix adhesions regulate communication between cells and the extracellular matrix. In matrix-secreting cells, fibrillar adhesions (FBs) containing high levels of α5β1 integrins and the tensin3 adaptor protein are essential for fibronectin (FN) fibrillogenesis. Here, we demonstrate that tensin3 binds to four helical regions (R3, R4, R8, and R11) of talin, the principal integrin activator. Structural analysis revealed the residues critical for the tensin3-talin interaction, and mutational analysis showed that talin R8 and R11 are essential for FB formation and FN fibrillogenesis. Cellular experiments demonstrate that tensin3 binding to talin not only regulates integrin activation, but also modulates tensin3's propensity to undergo liquid-liquid phase separation (LLPS). Formation of such LLPS condensates increased when cells were plated on soft substrates compared with stiff ones. This effect was abolished by blocking the interaction between tensin3 and talin. Our data suggest a model in which LLPS condensates provide a signaling platform involved in cellular responses to sudden changes in tissue mechanics.

Indexed as

Cell-Matrix JunctionsTalinTensins3T3 CellsAnimalsBinding SitesBiomolecular CondensatesFibronectinsHumansIntegrinsMiceMutationPhase SeparationProtein Interaction MapsProtein Structural ElementsFibronectinsIntegrinsTalinTensinsTLN1 protein, humanTNS3 protein, human

Identifiers

PMID41269158
PMCPMC12637021

What OpenQuestion holds

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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.