ArticleProceedings. Biological sciences2016
Myosin filament sliding through the Z-disc relates striated muscle fibre structure to function.
Article in Proceedings. Biological sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Feats of supercontractile strength: functional convergence of supercontracting muscle properties among hyoid musculature in chameleons.Proceedings. Biological sciences · 2025Article
- The effect of muscle ultrastructure on the force, displacement and work capacity of skeletal muscle.Journal of the Royal Society, Interface · 2024Article
- An optimized approach to study nanoscale sarcomere structure utilizing super-resolution microscopy with nanobodies.PloS one · 2024Article
- Structurally motivated models to explain the muscle's force-length relationship.Biophysical journal · 2023Article
- Sarcomere mechanics in the double-actin-overlap zone.Biophysical journal · 2023Article
- Ultrastructural and kinetic evidence support that thick filaments slide through the Z-disc.Journal of the Royal Society, Interface · 2022Article
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Investigating the effects of flexor tendon shortening on active range of motion after finger tendon repair.Anatomical record (Hoboken, N.J. : 2007) · 2022Article
- Actinin BioID reveals sarcomere crosstalk with oxidative metabolism through interactions with IGF2BP2.Cell reports · 2021Article
- Optical prediction of single muscle fiber force production using a combined biomechatronics and second harmonic generation imaging approach.Light, science & applications · 2018Article
- The active force-length relationship is invisible during extensive eccentric contractions in skinned skeletal muscle fibres.Proceedings. Biological sciences · 2017Article
- Importance of contraction history on muscle force of porcine urinary bladder smooth muscle.International urology and nephrology · 2017Article
- Porcine Stomach Smooth Muscle Force Depends on History-Effects.Frontiers in physiology · 2017Article
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4 authors.
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Abstract
Striated muscle contraction requires intricate interactions of microstructures. The classic textbook assumption that myosin filaments are compressed at the meshed Z-disc during striated muscle fibre contraction conflicts with experimental evidence. For example, myosin filaments are too stiff to be compressed sufficiently by the muscular force, and, unlike compressed springs, the muscle fibres do not restore their resting length after contractions to short lengths. Further, the dependence of a fibre's maximum contraction velocity on sarcomere length is unexplained to date. In this paper, we present a structurally consistent model of sarcomere contraction that reconciles these findings with the well-accepted sliding filament and crossbridge theories. The few required model parameters are taken from the literature or obtained from reasoning based on structural arguments. In our model, the transition from hexagonal to tetragonal actin filament arrangement near the Z-disc together with a thoughtful titin arrangement enables myosin filament sliding through the Z-disc. This sliding leads to swivelled crossbridges in the adjacent half-sarcomere that dampen contraction. With no fitting of parameters required, the model predicts straightforwardly the fibre's entire force-length behaviour and the dependence of the maximum contraction velocity on sarcomere length. Our model enables a structurally and functionally consistent view of the contractile machinery of the striated fibre with possible implications for muscle diseases and evolution.
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