Evidence map›Paper›PMID 42168662›Full record

ArticleScientific reports2026

Vimentin molecular linkages with nesprin-3 enhance nuclear deformations by cell geometric constraints.

Maxx Swoger, Minh Tri Ho Thanh, Renita Saldanha, Fitzroy J Byfield, Van Dam, Jessica Williamson, Bronson Frank, Heidi Hehnly, Daniel Conway, Alison E Patteson

Abstract read
In one paragraph

Article in Scientific reports, 2026. 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. Article
  2. Article
  3. Vimentin - Force regulator in confined environments.Current opinion in cell biology · 2025
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Maxx SwogerPhysics Department, Syracuse University, Syracuse, NY, USA.
Minh Tri Ho ThanhPhysics Department, Syracuse University, Syracuse, NY, USA.
Renita SaldanhaPhysics Department, Syracuse University, Syracuse, NY, USA.
Fitzroy J ByfieldDepartment of Physiology, University of Pennsylvania, Philadelphia, PA, USA.
Van DamPhysics Department, Syracuse University, Syracuse, NY, USA.
Jessica WilliamsonDepartment of Biomedical Engineering, Virginia Commonwealth University, Richmond, VA, USA.
Bronson FrankDepartment of Biomedical Engineering, The Ohio State University, Columbus, OH, USA.
Heidi HehnlyBioInspired Institute, Syracuse University, Syracuse, NY, USA.
Daniel ConwayDepartment of Biomedical Engineering, The Ohio State University, Columbus, OH, USA.
Alison E PattesonPhysics Department, Syracuse University, Syracuse, NY, USA. aepattes@syr.edu.

Funding

Cell junction and nuclear forces as mediators of epithelial cell homeostasisR35GM119617 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI Daniel E Conway · 2016 to 2026
$4.5M
Role of vimentin in mammalian cell motilityR35GM142963 · NIGMS · SYRACUSE UNIVERSITY · PI PATTESON, ALISON ELISE · 2021 to 2025
$2.1M
The relationship between Rab11-endosomes and the centrosome during divisionR01GM127621 · NIGMS · SYRACUSE UNIVERSITY · PI HEHNLY, HEIDI · 2018 to 2022
$1.8M
Cell cycle dependent mechanisms triggering lumen formation in vivoR01GM130874 · NIGMS · SYRACUSE UNIVERSITY · PI HEHNLY, HEIDI · 2021 to 2024
$1.2M
National Science Foundation CMMI 2238600NIGMS NIH HHS R01 GM127621NIGMS NIH HHS R01 GM130874NIGMS NIH HHS R35 GM119617NIGMS NIH HHS R35 GM142963NIH HHS R01GM-127621NIH HHS R35 GM119617NIH HHS R35GM142963
6 · The paper itself

Abstract

The nucleus is the organelle of the cell responsible for controlling protein expression, which has a direct effect on cellular biological functions. Here we show that the cytoskeletal protein vimentin plays an important role in increasing the amount of cell-generated forces transmitted to the cell nucleus, resulting in increased nuclear deformations in strongly polarized cells. Using micropatterned substrates to geometrically control cell shape in wild-type and vimentin-null cells, we show vimentin increases polarization and deformation of the cell nucleus. Loss of nesprin-3, which physically couples vimentin to the nuclear envelope, phenotypically copies the loss of vimentin, suggesting vimentin transmits forces to the cell nucleus through direct molecular linkages. Use of a Forster resonance energy transfer (FRET) sensor that binds to the nuclear envelope through lamin A/C suggests vimentin increases the tension on the nuclear envelope. Our results indicate that nuclear shape and deformation can be modified by the vimentin cytoskeleton and its specific crosslinks to the cell nucleus.

Indexed as

Cell NucleusNerve Tissue ProteinsNuclear ProteinsVimentinAnimalsCell ShapeCytoskeletonLamin Type AMembrane ProteinsMiceNuclear EnvelopeLamin Type AMembrane ProteinsNerve Tissue Proteinsnesprin-3 protein, mouseNuclear ProteinsVimentin

Identifiers

PMID42168662
PMCPMC13396528

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Registered trials

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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.