ArticleScientific reports2016
Regulation of actin catch-slip bonds with a RhoA-formin module.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Mechanoimmunology: past, present, and future perspectives.Mechanobiology in medicine · 2026Review
- Catch bond models may explain how force amplifies TCR signaling and antigen discrimination.Nature communications · 2023Article
- Stabilization of membrane topologies by proteinaceous remorin scaffolds.Nature communications · 2023Article
- Article
- MD Simulations on a Well-Built Docking Model Reveal Fine Mechanical Stability and Force-Dependent Dissociation of Mac-1/GPIbα Complex.Frontiers in molecular biosciences · 2021Article
- 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
- Dynamic bonds and their roles in mechanosensing.Current opinion in chemical biology · 2019Review
- Formin proteins in megakaryocytes and platelets: regulation of actin and microtubule dynamics.Platelets · 2019Review
- Mammalian Diaphanous-related formin-1 restricts early phases of influenza A/NWS/33 virus (H1N1) infection in LLC-MK2 cells by affecting cytoskeleton dynamics.Molecular and cellular biochemistry · 2018Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
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Abstract
The dynamic turnover of the actin cytoskeleton is regulated cooperatively by force and biochemical signaling. We previously demonstrated that actin depolymerization under force is governed by catch-slip bonds mediated by force-induced K113:E195 salt-bridges. Yet, the biochemical regulation as well as the functional significance of actin catch bonds has not been elucidated. Using AFM force-clamp experiments, we show that formin controlled by RhoA switches the actin catch-slip bonds to slip-only bonds. SMD simulations reveal that the force does not induce the K113:E195 interaction when formin binds to actin K118 and E117 residues located at the helical segment extending to K113. Actin catch-slip bonds are suppressed by single residue replacements K113E and E195K that interrupt the force-induced K113:E195 interaction; and this suppression is rescued by a K113E/E195K double mutant (E/K) restoring the interaction in the opposite orientation. These results support the biological significance of actin catch bonds, as they corroborate reported observations that RhoA and formin switch force-induced actin cytoskeleton alignment and that either K113E or E195K induces yeast cell growth defects rescued by E/K. Our study demonstrates how the mechano-regulation of actin dynamics is modulated by biochemical signaling molecules, and suggests that actin catch bonds may be important in cell functions.
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