Evidence map›Paper›PMID 35235449›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Vimentin intermediate filaments and filamentous actin form unexpected interpenetrating networks that redefine the cell cortex.

Huayin Wu, Yinan Shen, Suganya Sivagurunathan, Miriam Sarah Weber, Stephen A Adam, Jennifer H Shin, Jeffrey J Fredberg, Ohad Medalia, Robert Goldman, David A Weitz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  4. Review
  5. Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  6. Article
  7. Genome-wide single-cell perturbation screens with VIPerturb-seq.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. The intermediate filament protein GFAP regulates mitochondrial fission in astrocytes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
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  15. Review
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  19. Vimentin undergoes liquid-liquid phase separation to form droplets which wet and stabilize actin fibers.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. 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

10 authors at 4 institutions in 3 countries.

Huayin WuJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138.
Yinan ShenDepartment of Physics, Harvard University, Cambridge, MA 02138.
Suganya SivagurunathanDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611.ORCID 0000-0002-9778-5400
Miriam Sarah WeberDepartment of Biochemistry, University of Zurich, Zurich CH-8057, Switzerland.ORCID 0000-0003-2125-8222
Stephen A AdamDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611.ORCID 0000-0003-3444-7655
Jennifer H ShinDepartment of Mechanical Engineering, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.ORCID 0000-0001-8448-6236
Jeffrey J FredbergDepartment of Environmental Health, Harvard T. H. Chan School of Public Health, Boston, MA 02115.ORCID 0000-0002-7968-0920
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Zurich CH-8057, Switzerland.ORCID 0000-0003-0994-2937
Robert GoldmanDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611.
David A WeitzJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138.
Harvard University · USNorthwestern University · USUniversity of Zurich · CHKorea Advanced Institute of Science and Technology · KR

Funding

Structural basis of the specific protein-protein interactions underlying IF assemP01GM096971 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 2011 to 2021
$16.8M
Epithelial layer jamming in breast cancer cell migrationU01CA202123 · NCI · HARVARD SCHOOL OF PUBLIC HEALTH · PI FREDBERG, JEFFREY J · 2015 to 2019
$3.4M
Physics of bronchial epithelial unjammingR01HL148152 · NHLBI · HARVARD SCHOOL OF PUBLIC HEALTH · PI FREDBERG, JEFFREY J, PARK, JIN-AH · 2019 to 2022
$2.2M
NCI NIH HHS U01 CA202123NHLBI NIH HHS R01 HL148152NIGMS NIH HHS P01 GM096971
6 · The paper itself

Abstract

The cytoskeleton of eukaryotic cells is primarily composed of networks of filamentous proteins, F-actin, microtubules, and intermediate filaments. Interactions among the cytoskeletal components are important in determining cell structure and in regulating cell functions. For example, F-actin and microtubules work together to control cell shape and polarity, while the subcellular organization and transport of vimentin intermediate filament (VIF) networks depend on their interactions with microtubules. However, it is generally thought that F-actin and VIFs form two coexisting but separate networks that are independent due to observed differences in their spatial distribution and functions. In this paper, we present a closer investigation of both the structural and functional interplay between the F-actin and VIF cytoskeletal networks. We characterize the structure of VIFs and F-actin networks within the cell cortex using structured illumination microscopy and cryo-electron tomography. We find that VIFs and F-actin form an interpenetrating network (IPN) with interactions at multiple length scales, and VIFs are integral components of F-actin stress fibers. From measurements of recovery of cell contractility after transient stretching, we find that the IPN structure results in enhanced contractile forces and contributes to cell resilience. Studies of reconstituted networks and dynamic measurements in cells suggest direct and specific associations between VIFs and F-actin. From these results, we conclude that VIFs and F-actin work synergistically, both in their structure and in their function. These results profoundly alter our understanding of the contributions of the components of the cytoskeleton, particularly the interactions between intermediate filaments and F-actin.

Indexed as

Actin CytoskeletonActinsAnimalsBiopolymersCells, CulturedCytoplasmElectron Microscope TomographyIntermediate FilamentsMiceVimentinActinsBiopolymersVimentinVim protein, mousecell cortexhigh-resolution imaginginterpenetrating networks of F-actin and vimentin intermediate filamentstraction force microscopy

Identifiers

PMID35235449
PMCPMC8915831
OpenAlexW4220927067

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.