ArticleProceedings of the National Academy of Sciences of the United States of America2015
Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Impact of salt concentration and free magnesium on human beta-cardiac myosin reveal important details about the conserved mechanochemical mechanism.The Journal of biological chemistry · 2026Article
- The Problem with Inventing Molecular Mechanisms to Fit Thermodynamic Equations of Muscle.International journal of molecular sciences · 2023Article
- Theoretical efficiency limits and speed-efficiency trade-off in myosin motors.PLoS computational biology · 2023Article
- Insights into Muscle Contraction Derived from the Effects of Small-Molecular Actomyosin-Modulating Compounds.International journal of molecular sciences · 2022Article
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- Small Molecule RPI-194 Stabilizes Activated Troponin to Increase the Calcium Sensitivity of Striated Muscle Contraction.Frontiers in physiology · 2022Article
- Phase transformation-driven artificial muscle mimics the multifunctionality of avian wing muscle.Journal of the Royal Society, Interface · 2021Article
- Cardiac myosin contraction and mechanotransduction in health and disease.The Journal of biological chemistry · 2021Review
- Adhesion strength and contractility enable metastatic cells to become adurotactic.Cell reports · 2021Article
- Complexity in genetic cardiomyopathies and new approaches for mechanism-based precision medicine.The Journal of general physiology · 2021Article
- Evidence for S2 flexibility by direct visualization of quantum dot-labeled myosin heads and rods within smooth muscle myosin filaments moving on actin in vitro.The Journal of general physiology · 2021Article
- Synthesis and Evaluation of 4-Hydroxycoumarin Imines as Inhibitors of Class II Myosins.Journal of medicinal chemistry · 2020Article
- Microscopic heat pulses activate cardiac thin filaments.The Journal of general physiology · 2019Article
- Using the SpyTag SpyCatcher system to label smooth muscle myosin II filaments with a quantum dot on the regulatory light chain.Cytoskeleton (Hoboken, N.J.) · 2019Article
- Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin.Biophysical journal · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Five Alternative Myosin Converter Domains Influence Muscle Power, Stretch Activation, and Kinetics.Biophysical journal · 2018Article
- Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties.eLife · 2018Article
- A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Science advances · 2017Article
- A small-molecule modulator of cardiac myosin acts on multiple stages of the myosin chemomechanical cycle.The Journal of biological chemistry · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
It is not known which kinetic step in the acto-myosin ATPase cycle limits contraction speed in unloaded muscles (V0). Huxley's 1957 model [Huxley AF (1957) Prog Biophys Biophys Chem 7:255-318] predicts that V0 is limited by the rate that myosin detaches from actin. However, this does not explain why, as observed by Bárány [Bárány M (1967) J Gen Physiol 50(6, Suppl):197-218], V0 is linearly correlated with the maximal actin-activated ATPase rate (vmax), which is limited by the rate that myosin attaches strongly to actin. We have observed smooth muscle myosin filaments of different length and head number (N) moving over surface-attached F-actin in vitro. Fitting filament velocities (V) vs. N to a detachment-limited model using the myosin step size d=8 nm gave an ADP release rate 8.5-fold faster and ton (myosin's attached time) and r (duty ratio) ∼10-fold lower than previously reported. In contrast, these data were accurately fit to an attachment-limited model, V=N·v·d, over the range of N found in all muscle types. At nonphysiologically high N, V=L/ton rather than d/ton, where L is related to the length of myosin's subfragment 2. The attachment-limited model also fit well to the [ATP] dependence of V for myosin-rod cofilaments at three fixed N. Previously published V0 vs. vmax values for 24 different muscles were accurately fit to the attachment-limited model using widely accepted values for r and N, giving d=11.1 nm. Therefore, in contrast with Huxley's model, we conclude that V0 is limited by the actin-myosin attachment rate.
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