The molecular structural basis of the braking action of muscle

Authors

Hill, C., Kalakoutis, M., Arcidiacono, A., Fukutani, A., Narayanan, T., Brunello, E., Fusi, L., Irving, M.

Abstract

Skeletal muscles generate force and shortening through a structural powerstroke in actin-bound myosin motors linked to ATP hydrolysis, but they also act as brakes to resist stretching by an external load. The molecular structural basis of muscle braking has remained obscure. Here we show that muscle braking is driven both by structural changes in myosin motors and by distortion of the lattice of thick and thin filaments including their M-band and Z-disk connections. A strained motor conformation is established early during stretch, but force continues to increase as thin filaments are displaced from their symmetrical lattice positions, the lateral shear between thick filaments increases, and the lattice volume decreases. Moreover, whilst the motor conformation rapidly recovers after the stretch, the distortion of the filament lattice is largely maintained, storing the work done on the muscle during stretch and accounting for the residual force enhancement after stretch.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 02 Oct 2026.

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