ArticleProceedings of the National Academy of Sciences of the United States of America2011
Motion of myosin head domains during activation and force development in skeletal muscle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Piperine disrupts the OFF state of the resting thick filament of rat skeletal muscle, enhancing dynamic contractility in a fibre-type-dependent manner.The Journal of physiology · 2026Article
- Distinct distributions of myosin motor conformations during contraction of slow and fast skeletal muscle.The Journal of physiology · 2026Article
- Multi-omics Insight into Cardiac Myofibril Remodeling in Post-Prandial Burmese Pythons.bioRxiv : the preprint server for biology · 2026Article
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- An integrated picture of the structural pathways controlling the heart performance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural changes in troponin during activation of skeletal and heart muscle determined in situ by polarised fluorescence.Biophysical reviews · 2024Review
- Load-dependence of the activation of myosin filaments in heart muscle.The Journal of physiology · 2024Article
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- Dependence of myosin filament structure on intracellular calcium concentration in skeletal muscle.The Journal of general physiology · 2023Article
- Activation of skeletal muscle is controlled by a dual-filament mechano-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Muscle Mechanics and Thick Filament Activation: An Emerging Two-Way Interaction for the Vertebrate Striated Muscle Fine Regulation.International journal of molecular sciences · 2023Review
- Titin activates myosin filaments in skeletal muscle by switching from an extensible spring to a mechanical rectifier.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Background and roles: myosin in autoimmune diseases.Frontiers in cell and developmental biology · 2023Review
- Thick filament activation is different in fast- and slow-twitch skeletal muscle.The Journal of physiology · 2022Article
- Activation of the myosin motors in fast-twitch muscle of the mouse is controlled by mechano-sensing in the myosin filaments.The Journal of physiology · 2022Article
- Cooling intact and demembranated trabeculae from rat heart releases myosin motors from their inhibited conformation.The Journal of general physiology · 2022Article
- Myosin motors that cannot bind actin leave their folded OFF state on activation of skeletal muscle.The Journal of general physiology · 2021Article
- Myosin-based regulation of twitch and tetanic contractions in mammalian skeletal muscle.eLife · 2021Article
- Making waves: A proposed new role for myosin-binding protein C in regulating oscillatory contractions in vertebrate striated muscle.The Journal of general physiology · 2021Article
- Dependence of thick filament structure in relaxed mammalian skeletal muscle on temperature and interfilament spacing.The Journal of general physiology · 2021Article
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Authors and funding
9 authors.
Funding
Abstract
Muscle contraction is driven by a change in the structure of the head domain of myosin, the "working stroke" that pulls the actin filaments toward the midpoint of the myosin filaments. This movement of the myosin heads can be measured very precisely in intact muscle cells by X-ray interference, but until now this technique has not been applied to physiological activation and force generation following electrical stimulation of muscle cells. By using this approach, we show that the long axes of the myosin head domains are roughly parallel to the filaments in resting muscle, with their center of mass offset by approximately 7 nm from the C terminus of the head domain. The observed mass distribution matches that seen in electron micrographs of isolated myosin filaments in which the heads are folded back toward the filament midpoint. Following electrical stimulation, the heads move by approximately 10 nm away from the filament midpoint, in the opposite direction to the working stroke. The time course of this motion matches that of force generation, but is slower than the other structural changes in the myosin filaments on activation, including the loss of helical and axial order of the myosin heads and the change in periodicity of the filament backbone. The rate of force development is limited by that of attachment of myosin heads to actin in a conformation that is the same as that during steady-state isometric contraction; force generation in the actin-attached head is fast compared with the attachment step.
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