ArticleBiophysics and physicobiology2019
Millimeter-sized belt-like pattern formation of actin filaments in solution by interacting with surface myosin
Article in Biophysics and physicobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Elucidating chiral myosin-induced actin dynamics: From single-filament behavior to collective structures.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- An active matter model captures spatial dynamics of actomyosin oscillations in larval epithelial cells duringProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Transitions of the Bacteria-Fungi Microbiomes Associated with Different Life Cycle Stages of DinoflagellateMicroorganisms · 2025Article
- Emergence of diverse patterns driven by molecular motors in the motility assay.Cytoskeleton (Hoboken, N.J.) · 2024Article
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6 authors.
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Abstract
The movements of single actin filaments along a myosin-fixed glass surface were observed under a conventional fluorescence microscope. Although random at a low concentration, moving directions of filaments were aligned by the presence of over 1.0 mg/mL of unlabeled filaments. We found that actin filaments when at the intermediate concentrations ranging from 0.1 to 1.0 mg/mL, formed winding belt-like patterns and moved in a two-directional manner along the belts. These patterns were spread over a millimeter range and found to have bulged on the glass in a three-dimensional manner. Filaments did not get closer than about 37.5 nm to each other within each belt-pattern. The average width and the curvature radius of the pattern did not apparently change even when the range of actin concentrations was between 0.05 and 1.0 mg/mL or the sliding velocity between 1.2 and 3.2 μm/sec. However, when the length of filaments was shortened by ultrasonic treatments or the addition of gelsolin molecules, the curvature radius became small from 100 to 60 μm. These results indicate that this belt-forming nature of actin filaments may be due to some inter-filament interactions.
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