ArticleNature communications2024
Kinetic trapping organizes actin filaments within liquid-like protein droplets.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- A balance between nucleating and elongating actin filaments controls deformation of protein condensates.Science advances · 2026Article
- Nonequilibrium phases of a biomolecular condensate facilitated by enzyme activity.Soft matter · 2026Article
- Mechanochemical feedback between confinement and actin crosslinking drives the shape dynamics of liquid-like droplets.Nature communications · 2026Article
- Multiscale structure of chromatin condensates explains phase separation and material properties.Science (New York, N.Y.) · 2025Article
- Liquid-like condensates that bind actin promote assembly and bundling of actin filaments.Developmental cell · 2025Article
- The rheology and interfacial properties of biomolecular condensates.Biophysical reviews · 2025Review
- Nanocarriers for intracellular delivery of proteins in biomedical applications: strategies and recent advances.Journal of nanobiotechnology · 2024Review
- Growth-induced collective bending and kinetic trapping of cytoskeletal filaments.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Liquid-like condensates that bind actin drive filament polymerization and bundling.bioRxiv : the preprint server for biology · 2024Article
- Liquid-like condensates mediate competition between actin branching and bundling.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Several actin-binding proteins (ABPs) phase separate to form condensates capable of curating the actin network shapes. Here, we use computational modeling to understand the principles of actin network organization within VASP condensate droplets. Our simulations reveal that the different actin shapes, namely shells, rings, and mixture states are highly dependent on the kinetics of VASP-actin interactions, suggesting that they arise from kinetic trapping. Specifically, we show that reducing the residence time of VASP on actin filaments reduces degree of bundling, thereby promoting assembly of shells rather than rings. We validate the model predictions experimentally using a VASP-mutant with decreased bundling capability. Finally, we investigate the ring opening within deformed droplets and found that the sphere-to-ellipsoid transition is favored under a wide range of filament lengths while the ellipsoid-to-rod transition is only permitted when filaments have a specific range of lengths. Our findings highlight key mechanisms of actin organization within phase-separated ABPs.
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Registered trials
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.