ArticleScientific reports2016
Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 56 citations in OpenAlex.
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- Disease-associated mutations inbioRxiv : the preprint server for biology · 2026Article
- SimHS-AFMfit-MD: An Integrative Approach for Inferring Alpha-Actinin Atomic Conformational Dynamics.Nano letters · 2026Article
- Complementary cytoskeletal feedback loops control signal transduction excitability and cell polarity.Nature communications · 2025Article
- The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.International journal of molecular sciences · 2025Review
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
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- Troponin and a Myopathy-Linked Mutation inInternational journal of molecular sciences · 2023Article
- Physical pictures of rotation mechanisms of FFrontiers in molecular biosciences · 2023Article
- Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.Life science alliance · 2023Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- Coro1B and Coro1C regulate lamellipodia dynamics and cell motility by tuning branched actin turnover.The Journal of cell biology · 2022Article
- Distinct actin-tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes.iScience · 2022Article
- RTKN-1/Rhotekin shields endosome-associated F-actin from disassembly to ensure endocytic recycling.The Journal of cell biology · 2021Article
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- Article
- Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin.International journal of molecular sciences · 2020Article
- Long-Range and Directional Allostery of Actin Filaments Plays Important Roles in Various Cellular Activities.International journal of molecular sciences · 2020Review
- Biophysics at Waseda University.Biophysical reviews · 2020Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heavy meromyosin (HMM) of myosin II and cofilin each binds to actin filaments cooperatively and forms clusters along the filaments, but it is unknown whether the two cooperative bindings are correlated and what physiological roles they have. Fluorescence microscopy demonstrated that HMM-GFP and cofilin-mCherry each bound cooperatively to different parts of actin filaments when they were added simultaneously in 0.2 μM ATP, indicating that the two cooperative bindings are mutually exclusive. In 0.1 mM ATP, the motor domain of myosin (S1) strongly inhibited the formation of cofilin clusters along actin filaments. Under this condition, most actin protomers were unoccupied by S1 at any given moment, suggesting that transiently bound S1 alters the structure of actin filaments cooperatively and/or persistently to inhibit cofilin binding. Consistently, cosedimentation experiments using copolymers of actin and actin-S1 fusion protein demonstrated that the fusion protein affects the neighboring actin protomers, reducing their affinity for cofilin. In reciprocal experiments, cofilin-actin fusion protein reduced the affinity of neighboring actin protomers for S1. Thus, allosteric regulation by cooperative conformational changes of actin filaments contributes to mutually exclusive cooperative binding of myosin II and cofilin to actin filaments, and presumably to the differential localization of both proteins in cells.
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