ArticleProceedings of the National Academy of Sciences of the United States of America2008
Helical twist controls the thickness of F-actin bundles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 141 citations in OpenAlex.
- CaMKII generates actin bundle morphology and mechanics distinct from canonical bivalent cross-linkers.bioRxiv : the preprint server for biology · 2026Article
- Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.The Journal of cell biology · 2026Article
- Hierarchical Chiral Self-Assembly of Nanocylinders Composed of Sequence-Defined Mesogenic Dimers.Journal of the American Chemical Society · 2026Article
- Sensing the shape of a surface by tightly surface-bound filaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fascin structural plasticity mediates flexible actin bundle construction.Nature structural & molecular biology · 2025Article
- Stimuli-responsive self-regulating assembly of chiral colloids for robust size and shape control.Nature communications · 2024Article
- Fascin-induced bundling protects actin filaments from disassembly by cofilin.The Journal of cell biology · 2024Article
- Fascin structural plasticity mediates flexible actin bundle construction.bioRxiv : the preprint server for biology · 2024Article
- The actin cytoskeleton in hair bundle development and hearing loss.Hearing research · 2023Review
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- VASP localization to lipid bilayers induces polymerization driven actin bundle formation.Molecular biology of the cell · 2022Article
- Enhanced incorporation of subnanometer tags into cellular proteins for fluorescence nanoscopy via optimized genetic code expansion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A generalized Flory-Stockmayer kinetic theory of connectivity percolation and rigidity percolation of cytoskeletal networks.PLoS computational biology · 2022Article
- Visualising the cytoskeletal machinery in neuronal growth cones using cryo-electron tomography.Journal of cell science · 2022Article
- Arrested in Glass: Actin within Sophisticated Architectures of Biosilica in Sponges.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Actin crosslinker competition and sorting drive emergent GUV size-dependent actin network architecture.Communications biology · 2021Article
- Enhanced mechanosensing of cells in synthetic 3D matrix with controlled biophysical dynamics.Nature communications · 2021Article
- Regulation of Actin Bundle Mechanics and Structure by Intracellular Environmental Factors.Frontiers in physics · 2021Article
- Reconstitution of contractile actomyosin rings in vesicles.Nature communications · 2021Article
- Recapitulating Actin Module Organization in theInternational journal of molecular sciences · 2021Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the presence of condensing agents such as nonadsorbing polymer, multivalent counter ions, and specific bundling proteins, chiral biopolymers typically form bundles with a finite thickness, rather than phase-separating into a polymer-rich phase. Although short-range repulsive interactions or geometrical frustrations are thought to force the equilibrium bundle size to be limited, the precise mechanism is yet to be resolved. The importance of the tight control of biopolymer bundle size is illustrated by the ubiquitous cytoskeletal actin filament bundles that are crucial for the proper functioning of cells. Using an in vitro model system, we show that size control relies on a mismatch between the helical structure of individual actin filaments and the geometric packing constraints within bundles. Small rigid actin-binding proteins change the twist of filamentous actin (F-actin) in a concentration-dependent manner, resulting in small, well defined bundle thickness up to approximately 20 filaments, comparable to those found in filopodia. Other F-actin cross-linking proteins can subsequently link these small, well organized bundles into larger structures of several hundred filaments, comparable to those found in, for example, Drosophila bristles. The energetic tradeoff between filament twisting and cross-linker binding within a bundle is suggested as a fundamental mechanism by which cells can precisely adjust bundle size and strength.
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Registered trials
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.