ArticleProceedings of the National Academy of Sciences of the United States of America2025
Vimentin undergoes liquid-liquid phase separation to form droplets which wet and stabilize actin fibers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Centenarian SIRT6 variants elevate SIRT6 protein and enhance cellular senescence resistance.Research square · 2026Article
- A balance between nucleating and elongating actin filaments controls deformation of protein condensates.Science advances · 2026Article
- Plant NLRs are getting into higher-order architectures.The Plant journal : for cell and molecular biology · 2026Review
- Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Mechanobiological research fueling the advancement of mechanotherapy and mechanohealth.Mechanobiology in medicine · 2026Article
- Mechanochemical feedback between confinement and actin crosslinking drives the shape dynamics of liquid-like droplets.Nature communications · 2026Article
- Mechanomedicine: Present state and future promise.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Biomolecular phase separation in tumorigenesis: from aberrant condensates to therapeutic vulnerabilities.Molecular cancer · 2025Review
- 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 · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
The cytoskeleton is composed of F-actin, microtubules, and intermediate filaments (IFs). Vimentin is one of the most ubiquitous and well-studied IFs. It is involved in many activities including wound healing, tissue fibrosis, and cancer metastasis, all of which require rapid vimentin IF assembly. In this paper, we report that vimentin forms liquid condensates which appear to enable rapid filament growth. Given the transient nature of these droplets, we focus on properties of vimentin-Y117L, which has a point mutation that leads to formation of condensates but not IFs, enabling us to study these droplets in detail. The droplets dissolve under 1,6-Hexanediol treatment and under decreasing concentration, confirming that they are liquid, and phase separated. These condensates extensively wet actin stress fibers, rendering them resistant to actin-binding drugs and protecting them from depolymerization. We show similar behavior occurs in wild-type vimentin during its assembly into filaments.
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Registered trials
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