ArticleProceedings of the National Academy of Sciences of the United States of America2013
Actin depolymerization under force is governed by lysine 113:glutamic acid 195-mediated catch-slip bonds.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
40 citing papers in PubMed.
- Cytoskeletal prestress homeostasis is a biological principle that governs living cell structure and function.Mechanobiology in medicine · 2026Review
- Mechanoimmunology: past, present, and future perspectives.Mechanobiology in medicine · 2026Review
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- Catch bond models may explain how force amplifies TCR signaling and antigen discrimination.Nature communications · 2023Article
- Catch bond-inspired hydrogels with repeatable and loading rate-sensitive specific adhesion.Bioactive materials · 2023Article
- Recombinant FimH Adhesin Demonstrates How the Allosteric Catch Bond Mechanism Can Support Fast and Strong Bacterial Attachment in the Absence of Shear.Journal of molecular biology · 2022Article
- Biomechanical microenvironment in peripheral nerve regeneration: from pathophysiological understanding to tissue engineering development.Theranostics · 2022Review
- Mechanotransduction as a major driver of cell behaviour: mechanisms, and relevance to cell organization and future research.Open biology · 2021Review
- Editorial: Understanding molecular interactions that underpin vascular mechanobiology.APL bioengineering · 2021Article
- Biomechanics of T Cell Dysfunctions in Chronic Diseases.Frontiers in immunology · 2021Review
- Mechanosensation in traumatic brain injury.Neurobiology of disease · 2021Review
- Mechanochemical coupling of formin-induced actin interaction at the level of single molecular complex.Biomechanics and modeling in mechanobiology · 2020Article
- From cellular to molecular mechanobiology.APL bioengineering · 2020Article
- Review
- When Stiffness Matters: Mechanosensing in Heart Development and Disease.Frontiers in cell and developmental biology · 2020Review
- Dynamic bonds and their roles in mechanosensing.Current opinion in chemical biology · 2019Review
- Mechanosensing through immunoreceptors.Nature immunology · 2019Article
- Energy-Mediated Machinery Drives Cellular Mechanical Allostasis.Advanced materials (Deerfield Beach, Fla.) · 2019Article
- Tensile and compressive force regulation on cell mechanosensing.Biophysical reviews · 2019Review
- Force-history dependence and cyclic mechanical reinforcement of actin filaments at the single molecular level.Journal of cell science · 2019Article
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Authors and funding
10 authors.
Funding
Abstract
As a key element in the cytoskeleton, actin filaments are highly dynamic structures that constantly sustain forces. However, the fundamental question of how force regulates actin dynamics is unclear. Using atomic force microscopy force-clamp experiments, we show that tensile force regulates G-actin/G-actin and G-actin/F-actin dissociation kinetics by prolonging bond lifetimes (catch bonds) at a low force range and by shortening bond lifetimes (slip bonds) beyond a threshold. Steered molecular dynamics simulations reveal force-induced formation of new interactions that include a lysine 113(K113):glutamic acid 195 (E195) salt bridge between actin subunits, thus suggesting a molecular basis for actin catch-slip bonds. This structural mechanism is supported by the suppression of the catch bonds by the single-residue replacements K113 to serine (K113S) and E195 to serine (E195S) on yeast actin. These results demonstrate and provide a structural explanation for actin catch-slip bonds, which may provide a mechanoregulatory mechanism to control cell functions by regulating the depolymerization kinetics of force-bearing actin filaments throughout the cytoskeleton.
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Registered trials
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