ArticleProceedings of the National Academy of Sciences of the United States of America2017
Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 77 citations in OpenAlex.
- Zyxin and LPP differ in their sensing of strained actin filaments at tricellular junctions.bioRxiv : the preprint server for biology · 2026Article
- Profilin promotes lamellipodium protrusion by tuning the antagonistic activities of capping protein and VASP.Nature communications · 2026Article
- Actomyosin-dependent assembly of the mechanosensitive machinery from adherens junctions triggers actin polymerization and organization.Science advances · 2026Article
- ADPact: A versatile sensor for ADP-F-actin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Liquid-like condensates that bind actin promote assembly and bundling of actin filaments.Developmental cell · 2025Article
- Supramolecular fibrillation in coacervates and other confined systems towards biomimetic function.Communications chemistry · 2024Review
- Spa2 remodels ADP-actin via molecular condensation under glucose starvation.Nature communications · 2024Article
- Force-activated zyxin assemblies coordinate actin nucleation and crosslinking to orchestrate stress fiber repair.bioRxiv : the preprint server for biology · 2024Article
- Liquid-like condensates mediate competition between actin branching and bundling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multi-monoubiquitylation controls VASP-mediated actin dynamics.Journal of cell science · 2024Article
- Enabled primarily controls filopodial morphology, not actin organization, in the TSM1 growth cone inMolecular biology of the cell · 2023Article
- Review
- Liquid-like condensates mediate competition between actin branching and bundling.bioRxiv : the preprint server for biology · 2023Article
- A new view of axon growth and guidance grounded in the stochastic dynamics of actin networks.Open biology · 2023Article
- Liquid-like VASP condensates drive actin polymerization and dynamic bundling.Nature physics · 2023Article
- Article
- Ena/VASP clustering at microspike tips involves lamellipodin but not I-BAR proteins, and absolutely requires unconventional myosin-X.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions.Science advances · 2022Article
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 2022Review
- VASP localization to lipid bilayers induces polymerization driven actin bundle formation.Molecular biology of the cell · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ena/VASP proteins act as actin polymerases that drive the processive elongation of filament barbed ends in membrane protrusions or at the surface of bacterial pathogens. Based on previous analyses of fast and slow elongating VASP proteins by in vitro total internal reflection fluorescence microscopy (TIRFM) and kinetic and thermodynamic measurements, we established a kinetic model of Ena/VASP-mediated actin filament elongation. At steady state, it entails that tetrameric VASP uses one of its arms to processively track growing filament barbed ends while three G-actin-binding sites (GABs) on other arms are available to recruit and deliver monomers to the filament tip, suggesting that VASP operates as a single tetramer in solution or when clustered on a surface, albeit processivity and resistance toward capping protein (CP) differ dramatically between both conditions. Here, we tested the model by variation of the oligomerization state and by increase of the number of GABs on individual polypeptide chains. In excellent agreement with model predictions, we show that in solution the rates of filament elongation directly correlate with the number of free GABs. Strikingly, however, irrespective of the oligomerization state or presence of additional GABs, filament elongation on a surface invariably proceeded with the same rate as with the VASP tetramer, demonstrating that adjacent VASP molecules synergize in the elongation of a single filament. Additionally, we reveal that actin ATP hydrolysis is not required for VASP-mediated filament assembly. Finally, we show evidence for the requirement of VASP to form tetramers and provide an amended model of processive VASP-mediated actin assembly in clustered arrays.
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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.