ArticleBiophysical journal2021
Actin bundle architecture and mechanics regulate myosin II force generation.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Decoding Cytoskeletal Mechanobiology with Tunable Microenvironments.ACS biomaterials science & engineering · 2026Article
- Stress-Induced Mechanical Memory in Respiratory Mucus: Anisotropy, Network Reorganization, and Directional Transport.bioRxiv : the preprint server for biology · 2026Article
- Feedback between filament spacing, crosslinker binding, and self-organization in cytoskeletal bundles.bioRxiv : the preprint server for biology · 2026Article
- Crosslinked F-actin networks regulate load-dependent energy conversion.Communications biology · 2026Article
- 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
- Review
- Micron-resolution fiber mapping in histology independent of sample preparation.Nature communications · 2025Article
- Micron-resolution fiber mapping in histology independent of sample preparation.bioRxiv : the preprint server for biology · 2025Article
- Article
- Direct detection of deformation modes on varying length scales in active biopolymer networks.bioRxiv : the preprint server for biology · 2025Article
- Stabilization of adhesions controls F-actin architecture in mechanotransduction.Communications materials · 2025Article
- Self-organized spatial targeting of contractile actomyosin rings for synthetic cell division.Nature communications · 2024Article
- The structure and mechanics of the cell cortex depend on the location and adhesion state.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanical and biochemical feedback combine to generate complex contractile oscillations in cytokinesis.Current biology : CB · 2024Article
- Composite branched and linear F-actin maximize myosin-induced membrane shape changes in a biomimetic cell model.Communications biology · 2024Article
- F-actin architecture determines the conversion of chemical energy into mechanical work.Nature communications · 2024Article
- Drebrin is Required for Myosin-facilitated Actin Cytoskeletal Remodeling during Pulmonary Alveolar Development.American journal of respiratory cell and molecular biology · 2024Article
- A modified motor-clutch model reveals that neuronal growth cones respond faster to soft substrates.Molecular biology of the cell · 2024Article
- Deep learning strategy for small dataset from atomic force microscopy mechano-imaging on macrophages phenotypes.Frontiers in bioengineering and biotechnology · 2023Article
- F-actin architecture determines constraints on myosin thick filament motion.Nature communications · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The actin cytoskeleton is a soft, structural material that underlies biological processes such as cell division, motility, and cargo transport. The cross-linked actin filaments self-organize into a myriad of architectures, from disordered meshworks to ordered bundles, which are hypothesized to control the actomyosin force generation that regulates cell migration, shape, and adhesion. Here, we use fluorescence microscopy and simulations to investigate how actin bundle architectures with varying polarity, spacing, and rigidity impact myosin II dynamics and force generation. Microscopy reveals that mixed-polarity bundles formed by rigid cross-linkers support slow, bidirectional myosin II filament motion, punctuated by periods of stalled motion. Simulations reveal that these locations of stalled myosin motion correspond to sustained, high forces in regions of balanced actin filament polarity. By contrast, mixed-polarity bundles formed by compliant, large cross-linkers support fast, bidirectional motion with no traps. Simulations indicate that trap duration is directly related to force magnitude and that the observed increased velocity corresponds to lower forces resulting from both the increased bundle compliance and filament spacing. Our results indicate that the microstructures of actin assemblies regulate the dynamics and magnitude of myosin II forces, highlighting the importance of architecture and mechanics in regulating forces in biological materials.
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