ArticleProceedings of the National Academy of Sciences of the United States of America2007
Skeletal muscle resists stretch by rapid binding of the second motor domain of myosin to actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 118 citations in OpenAlex.
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Stretch-shortening cycles mitigate single muscle fibre power deficits following a two-week immobilization of the rat hindlimb.Journal of muscle research and cell motility · 2026Article
- Monolithic electrostatic actuators with independent stiffness modulation.Nature communications · 2025Article
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.Frontiers in physiology · 2025Article
- Reduced cardiovascular and metabolic responses during eccentric stepping exercise: A pilot study.Physiological reports · 2024Article
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- Cooperativity of myosin II motors in the non-regulated and regulated thin filaments investigated with high-speed AFM.The Journal of general physiology · 2023Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- Article
- Myosin motors that cannot bind actin leave their folded OFF state on activation of skeletal muscle.The Journal of general physiology · 2021Article
- Effect of Active Lengthening and Shortening on Small-Angle X-ray Reflections in Skinned Skeletal Muscle Fibres.International journal of molecular sciences · 2021Article
- A reverse stroke characterizes the force generation of cardiac myofilaments, leading to an understanding of heart function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
- Evidence for Muscle Cell-Based Mechanisms of Enhanced Performance in Stretch-Shortening Cycle in Skeletal Muscle.Frontiers in physiology · 2020Review
- Insights into Actin-Myosin Interactions within Muscle from 3D Electron Microscopy.International journal of molecular sciences · 2019Review
- On the Shape of the Force-Velocity Relationship in Skeletal Muscles: The Linear, the Hyperbolic, and the Double-Hyperbolic.Frontiers in physiology · 2019Review
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Active shortening protects against stretch-induced force deficits in human skeletal muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2017Article
- Myosin filament activation in the heart is tuned to the mechanical task.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
A shortening muscle is a machine that converts metabolic energy into mechanical work, but, when a muscle is stretched, it acts as a brake, generating a high resistive force at low metabolic cost. The braking action of muscle can be activated with remarkable speed, as when the leg extensor muscles rapidly decelerate the body at the end of a jump. Here we used time-resolved x-ray and mechanical measurements on isolated muscle cells to elucidate the molecular basis of muscle braking and its rapid control. We show that a stretch of only 5 nm between each overlapping set of myosin and actin filaments in a muscle sarcomere is sufficient to double the number of myosin motors attached to actin within a few milliseconds. Each myosin molecule has two motor domains, only one of which is attached to actin during shortening or activation at constant length. A stretch strains the attached motor domain, and we propose that combined steric and mechanical coupling between the two domains promotes attachment of the second motor domain. This mechanism allows skeletal muscle to resist external stretch without increasing the force per motor and provides an answer to the longstanding question of the functional role of the dimeric structure of muscle myosin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.