ArticleThe Journal of cell biology2011
Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 165 papers.
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Who cites it
165 citing papers in PubMed, 345 citations in OpenAlex.
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- Viscous drag-induced self-regeneration of laser-dissected actin stress fibers: A potential mechanism for mechanical memory.Mechanobiology in medicine · 2026Article
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- Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025Review
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- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Structural and functional mechanisms of actin isoforms.The FEBS journal · 2025Review
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- Cracked actin filaments as mechanosensitive receptors.Biophysical journal · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.The Journal of cell biology · 2024Article
- Single-pericyte nanomechanics measured by contraction cytometry.APL bioengineering · 2024Article
- Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.bioRxiv : the preprint server for biology · 2024Article
- Myosin-induced F-actin fragmentation facilitates contraction of actin networks.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Plakophilin 4 controls the spatio-temporal activity of RhoA at adherens junctions to promote cortical actin ring formation and tissue tension.Cellular and molecular life sciences : CMLS · 2024Article
105 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular and extracellular mechanical forces affect the structure and dynamics of the actin cytoskeleton. However, the underlying molecular and biophysical mechanisms, including how mechanical forces are sensed, are largely unknown. Actin-depolymerizing factor/cofilin proteins are actin-modulating proteins that are ubiquitously distributed in eukaryotes, and they are the most likely candidate as proteins to drive stress fiber disassembly in response to changes in tension in the fiber. In this study, we propose a novel hypothesis that tension in an actin filament prevents the filament from being severed by cofilin. To test this, we placed single actin filaments under tension using optical tweezers. When a fiber was tensed, it was severed after the application of cofilin with a significantly larger delay in comparison with control filaments suspended in solution. The binding rate of cofilin to an actin bundle decreased when the bundle was tensed. These results suggest that tension in an actin filament reduces the cofilin binding, resulting in a decrease in its effective severing activity.
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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.