ArticleProceedings of the National Academy of Sciences of the United States of America2023
Activation of skeletal muscle is controlled by a dual-filament mechano-sensing mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 28 citations in OpenAlex.
- 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
- Subsarcomeric regulation of thin and thick filaments in skeletal muscle myofibrils.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanisms of protein degradation in atrophying muscles: What have we learned during the past decade?The Journal of biological chemistry · 2026Review
- Comparison of Predicted X-Ray Fiber Diffraction Patterns from All-Atom and Coarse-Grained Actin Filament Models Under Nonuniform Strain.International journal of molecular sciences · 2025Article
- Cardiac myosin-binding protein-C acts as a tunable load sensor to regulate afterload dependence of ventricular function.American journal of physiology. Heart and circulatory physiology · 2025Article
- Theoretical treatment of tension transients in muscle following sudden changes in orthophosphate concentration: implications for energy transduction.Journal of muscle research and cell motility · 2025Article
- A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Various challenges in understanding the thick filaments, within and outside skeletal and cardiac muscles.Biophysical reviews · 2025Article
- Interplay between extracellular matrix mechanics and cell function in mechanobiology.Current opinion in biomedical engineering · 2025Article
- Consecutive SSCs increase the SSC effect in skinned rat muscle fibres.Pflugers Archiv : European journal of physiology · 2025Article
- A combined experimental and computational analysis of mantATP turnover in skinned muscle fibers.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Myosin binding protein-C modulates loaded sarcomere shortening in rodent permeabilized cardiac myocytes.The Journal of general physiology · 2025Article
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Association of serum magnesium and calcium with metabolic syndrome: a cross-sectional study from the Qatar-biobank.Nutrition & metabolism · 2025Article
- Functional control of myosin motors in the cardiac cycle.Nature reviews. Cardiology · 2025Review
- A FRET assay to quantitate levels of the human β-cardiac myosin interacting heads motif based on its near-atomic resolution structure.bioRxiv : the preprint server for biology · 2024Article
- 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
- Post-translational modifications of vertebrate striated muscle myosin heavy chains.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Load-dependence of the activation of myosin filaments in heart muscle.The Journal of physiology · 2024Article
- Structural changes in troponin during activation of skeletal and heart muscle determined in situ by polarised fluorescence.Biophysical reviews · 2024Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
Abstract
Contraction of skeletal muscle is triggered by a transient rise in intracellular calcium concentration leading to a structural change in the actin-containing thin filaments that allows binding of myosin motors from the thick filaments. Most myosin motors are unavailable for actin binding in resting muscle because they are folded back against the thick filament backbone. Release of the folded motors is triggered by thick filament stress, implying a positive feedback loop in the thick filaments. However, it was unclear how thin and thick filament activation mechanisms are coordinated, partly because most previous studies of the thin filament regulation were conducted at low temperatures where the thick filament mechanisms are inhibited. Here, we use probes on both troponin in the thin filaments and myosin in the thick filaments to monitor the activation states of both filaments in near-physiological conditions. We characterize those activation states both in the steady state, using conventional titrations with calcium buffers, and during activation on the physiological timescale, using calcium jumps produced by photolysis of caged calcium. The results reveal three activation states of the thin filament in the intact filament lattice of a muscle cell that are analogous to those proposed previously from studies on isolated proteins. We characterize the rates of the transitions between these states in relation to thick filament mechano-sensing and show how thin- and thick-filament-based mechanisms are coupled by two positive feedback loops that switch on both filaments to achieve rapid cooperative activation of skeletal muscle.
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