Evidence map›Paper›PMID 42102206›Full record

ArticleScience advances2026

Reconstituted nascent adhesion condensates drive actin polymerization on supported lipid bilayers.

Arsenii Hordeichyk, Kristian A T Pajanonot, Chiao-Peng Hsu, Timon Nast-Kolb, Lukas J Neumann, Reinhard Fässler, Andreas R Bausch

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Arsenii HordeichykHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0009-0004-7402-1354
Kristian A T PajanonotHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0009-0007-1966-3743
Chiao-Peng HsuHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0000-0002-6994-7708
Timon Nast-KolbHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0000-0002-2706-6486
Lukas J NeumannHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0000-0002-0200-4545
Reinhard FässlerHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0000-0002-0145-6937
Andreas R BauschHeinz Nixdorf Chair in Biophysical Engineering of Living Matter, Center for Functional Protein Assemblies, Center for Organoid Systems, Department of Bioscience, Technical University of Munich, Technical University of Munich School of Natural Sciences, Garching 85748, Germany.ORCID 0000-0002-4608-9544

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nascent adhesions are early integrin-based assemblies that couple the extracellular matrix to the actin cytoskeleton and mature into focal adhesions. Many nascent-adhesion proteins interact through weak, multivalent contacts, suggesting that liquid-like organization may contribute to adhesion assembly. However, how phase separation shapes actin polymerization and organization remains unclear. Here, we compare two vasodilator-stimulated phosphoprotein (VASP)-recruiting adaptor proteins, zyxin and vinculin, to determine how adaptor identity tunes condensate properties and actin coupling. Both zyxin-VASP and vinculin-VASP assemblies drive integrin clustering and support actin filament growth. Notably, zyxin-VASP condensates remain fluid and redistribute along newly formed actin bundles, whereas vinculin-VASP condensates are more rigid and fail to spread along actin despite sustaining polymerization. These results suggest that differential VASP recruitment can modulate condensate properties and actin architecture, providing a potential mechanism for the maturation of nascent adhesions into focal adhesions.

Indexed as

ActinsLipid BilayersActin CytoskeletonAnimalsCell AdhesionCell Adhesion MoleculesFocal AdhesionsHumansIntegrinsMicrofilament ProteinsPhosphoproteinsPolymerizationVasodilator-Stimulated PhosphoproteinVinculinZyxinActinsCell Adhesion MoleculesIntegrinsLipid BilayersMicrofilament ProteinsPhosphoproteinsVinculinZyxin

Identifiers

PMID42102206
PMCPMC13155341

What Socratic 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 Socratic graph.