ArticleMolecular biology of the cell2022
VASP localization to lipid bilayers induces polymerization driven actin bundle formation.
Article in Molecular biology of the cell, 2022. 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, 10 citations in OpenAlex.
- Simulations show increased lipid interdigitation in transmembrane coupling of protein condensates.bioRxiv : the preprint server for biology · 2026Article
- RBM39 upregulation promotes ostium re-obstruction after endoscopic endonasal dacryocystorhinostomy (En-DCR).BMC molecular and cell biology · 2026Article
- Reconstituted nascent adhesion condensates drive actin polymerization on supported lipid bilayers.Science advances · 2026Article
- Force Transmission by Minimal Focal Adhesion Complexes Induces Synthetic Cell Deformation.ACS synthetic biology · 2026Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Benefits and challenges of reconstituting the actin cortex.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Membrane Ruffles: Composition, Function, Formation and Visualization.International journal of molecular sciences · 2024Review
- Liquid-like condensates mediate competition between actin branching and bundling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin bundles constitute important cytoskeleton structures and enable a scaffold for force transmission inside cells. Actin bundles are formed by proteins, with multiple F-actin binding domains cross-linking actin filaments to each other. Vasodilator-stimulated phosphoprotein (VASP) has mostly been reported as an actin elongator, but it has been shown to be a bundling protein as well and is found in bundled actin structures at filopodia and adhesion sites. Based on in vitro experiments, it remains unclear when and how VASP can act as an actin bundler or elongator. Here we demonstrate that VASP bound to membranes facilitates the formation of large actin bundles during polymerization. The alignment by polymerization requires the fluidity of the lipid bilayers. The mobility within the bilayer enables VASP to bind to filaments and capture and track growing barbed ends. VASP itself phase separates into a protein-enriched phase on the bilayer. This VASP-rich phase nucleates and accumulates at bundles during polymerization, which in turn leads to a reorganization of the underlying lipid bilayer. Our findings demonstrate that the nature of VASP localization is decisive for its function. The up-concentration based on VASP's affinity to actin during polymerization enables it to simultaneously fulfill the function of an elongator and a bundler.
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