ArticleProceedings of the National Academy of Sciences of the United States of America2012
F-actin buckling coordinates contractility and severing in a biomimetic actomyosin cortex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 204 papers.
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204 citing papers in PubMed, 428 citations in OpenAlex.
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- Differential activity of nonmuscle myosin IIA and IIB isoforms generates a dynamic actomyosin network in a concentration-dependent manner.The Journal of biological chemistry · 2026Article
- Crosslinked F-actin networks regulate load-dependent energy conversion.Communications biology · 2026Article
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- Septins buffer actomyosin forces to protect the nucleus from genotoxic mechanical stress.bioRxiv : the preprint server for biology · 2026Article
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- Quantitative Signatures of Disassembly Mechanisms Modulating Filament and Bundle Assembly in a Shared Pool.bioRxiv : the preprint server for biology · 2025Article
- Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 2025Article
- Adhesion strength, cell packing density and cell surface buckling in pericellular matrix-mediated tissue cohesion.Development (Cambridge, England) · 2025Article
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144 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
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Abstract
Here we develop a minimal model of the cell actomyosin cortex by forming a quasi-2D cross-linked filamentous actin (F-actin) network adhered to a model cell membrane and contracted by myosin thick filaments. Myosin motors generate both compressive and tensile stresses on F-actin and consequently induce large bending fluctuations, which reduces their effective persistence length to <1 μm. Over a large range of conditions, we show the extent of network contraction corresponds exactly to the extent of individual F-actin shortening via buckling. This demonstrates an essential role of buckling in breaking the symmetry between tensile and compressive stresses to facilitate mesoscale network contraction of up to 80% strain. Portions of buckled F-actin with a radius of curvature ~300 nm are prone to severing and thus compressive stresses mechanically coordinate contractility with F-actin severing, the initial step of F-actin turnover. Finally, the F-actin curvature acquired by myosin-induced stresses can be further constrained by adhesion of the network to a membrane, accelerating filament severing but inhibiting the long-range transmission of the stresses necessary for network contractility. Thus, the extent of membrane adhesion can regulate the coupling between network contraction and F-actin severing. These data demonstrate the essential role of the nonlinear response of F-actin to compressive stresses in potentiating both myosin-mediated contractility and filament severing. This may serve as a general mechanism to mechanically coordinate contractility and cortical dynamics across diverse actomyosin assemblies in smooth muscle and nonmuscle cells.
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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.