ArticleScientific reports2016
Early nucleation events in the polymerization of actin, probed by time-resolved small-angle x-ray scattering.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- On the Assembly of Actin Polymerization-Powered Motors.Macromolecular rapid communications · 2026Article
- Agent-based modelling of the early stages of actin polymerisation required to drive endocytosis in Saccharomyces cerevisiae.Scientific reports · 2025Article
- A structural model of the profilin-formin pacemaker system for actin filament elongation.Scientific reports · 2022Article
- Mechanism of actin filament nucleation.Biophysical journal · 2021Article
- GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation.The Journal of cell biology · 2021Article
- Insights into Actin Polymerization and Nucleation Using a Coarse-Grained Model.Biophysical journal · 2020Article
- Towards a structural understanding of the remodeling of the actin cytoskeleton.Seminars in cell & developmental biology · 2020Review
- Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020Article
- Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering.Biophysical reviews · 2019Review
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
- Apicomplexan actin polymerization depends on nucleation.Scientific reports · 2017Article
- Article
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3 authors.
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Abstract
Nucleators generating new F-actin filaments play important roles in cell activities. Detailed information concerning the events involved in nucleation of actin alone in vitro is fundamental to understanding these processes, but such information has been hard to come by. We addressed the early process of salt-induced polymerization of actin using the time-resolved synchrotron small-angle X-ray scattering (SAXS). Actin molecules in low salt solution maintain a monomeric state by an electrostatic repulsive force between molecules. On mixing with salts, the repulsive force was rapidly screened, causing an immediate formation of many of non-polymerizable dimers. SAXS kinetic analysis revealed that tetramerization gives the highest energetic barrier to further polymerization, and the major nucleation is the formation of helical tetramers. Filaments start to grow rapidly with the formation of pentamers. These findings suggest an acceleration mechanism of actin assembly by a variety of nucleators in cells.
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