ArticleProceedings of the National Academy of Sciences of the United States of America2019
Cofilin drives rapid turnover and fluidization of entangled F-actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 51 citations in OpenAlex.
- Rapid actin filament turnover maintains cortical connectivity while allowing for cell cortex deformation and flow.bioRxiv : the preprint server for biology · 2026Article
- Deep-DPC: Deep learning-assisted label-free temporal imaging discovery of anti-fibrotic compounds by controlling cell morphology.Journal of advanced research · 2025Article
- Fast Actin Disassembly and Fimbrin Mechanosensitivity Support Rapid Turnover in a Model of Clathrin-Mediated Endocytosis.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025Review
- Effects of SIPA1L1 on trabecular meshwork extracellular matrix protein accumulation and cellular phagocytosis in POAG.JCI insight · 2024Article
- Mechanical power is maximized during contractile ring-like formation in a biomimetic dividing cell model.Nature communications · 2024Article
- Blebology: principles of bleb-based migration.Trends in cell biology · 2024Review
- F-actin architecture determines the conversion of chemical energy into mechanical work.Nature communications · 2024Article
- Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change.European journal of cell biology · 2024Article
- Coronin-1 promotes directional cell rearrangement in Drosophila wing epithelium.Cell structure and function · 2023Article
- Worm blobs as entangled living polymers: from topological active matter to flexible soft robot collectives.Soft matter · 2023Review
- Septin11 promotes hepatocellular carcinoma cell motility by activating RhoA to regulate cytoskeleton and cell adhesion.Cell death & disease · 2023Article
- A tug of war between filament treadmilling and myosin induced contractility generates actin rings.eLife · 2022Article
- Actomyosin-Driven Division of a Synthetic Cell.ACS synthetic biology · 2022Review
- Multiscale architecture: Mechanics of composite cytoskeletal networks.Biophysics reviews · 2022Review
- Avian Hepatitis E Virus ORF2 Protein Interacts with Rap1b to Induce Cytoskeleton Rearrangement That Facilitates Virus Internalization.Microbiology spectrum · 2022Article
- Molecular and structural basis of actin filament severing by ADF/cofilin.Computational and structural biotechnology journal · 2022Article
- Efficient T Cell Migration and Activation Require L-Plastin.Frontiers in immunology · 2022Review
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The shape of most animal cells is controlled by the actin cortex, a thin network of dynamic actin filaments (F-actin) situated just beneath the plasma membrane. The cortex is held far from equilibrium by both active stresses and polymer turnover: Molecular motors drive deformations required for cell morphogenesis, while actin-filament disassembly dynamics relax stress and facilitate cortical remodeling. While many aspects of actin-cortex mechanics are well characterized, a mechanistic understanding of how nonequilibrium actin turnover contributes to stress relaxation is still lacking. To address this, we developed a reconstituted in vitro system of entangled F-actin, wherein the steady-state length and turnover rate of F-actin are controlled by the actin regulatory proteins cofilin, profilin, and formin, which sever, recycle, and assemble filaments, respectively. Cofilin-mediated severing accelerates the turnover and spatial reorganization of F-actin, without significant changes to filament length. We demonstrate that cofilin-mediated severing is a single-timescale mode of stress relaxation that tunes the low-frequency viscosity over two orders of magnitude. These findings serve as the foundation for understanding the mechanics of more physiological F-actin networks with turnover and inform an updated microscopic model of single-filament turnover. They also demonstrate that polymer activity, in the form of ATP hydrolysis on F-actin coupled to nucleotide-dependent cofilin binding, is sufficient to generate a form of active matter wherein asymmetric filament disassembly preserves filament number despite sustained severing.
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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.