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Myosin Cross-Bridge Behaviour in Contracting Muscle—The T1 Curve of Huxley and Simmons (1971) Revisited
Open AccessEditorial

Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview

by John Squire 1,2
1
Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol BS8 1TD, UK
2
Department of Surgery and Cancer, Faculty of Medicine, Imperial College London, London SW7 2BZ, UK
Int. J. Mol. Sci. 2019, 20(22), 5715; https://doi.org/10.3390/ijms20225715
Received: 11 October 2019 / Accepted: 15 October 2019 / Published: 14 November 2019
(This article belongs to the Special Issue The Actin-Myosin Interaction in Muscle)
Muscular contraction is a fundamental phenomenon in all animals; without it life as we know it would be impossible. The basic mechanism in muscle, including heart muscle, involves the interaction of the protein filaments myosin and actin. Motility in all cells is also partly based on similar interactions of actin filaments with non-muscle myosins. Early studies of muscle contraction have informed later studies of these cellular actin-myosin systems. In muscles, projections on the myosin filaments, the so-called myosin heads or cross-bridges, interact with the nearby actin filaments and, in a mechanism powered by ATP-hydrolysis, they move the actin filaments past them in a kind of cyclic rowing action to produce the macroscopic muscular movements of which we are all aware. In this special issue the papers and reviews address different aspects of the actin-myosin interaction in muscle as studied by a plethora of complementary techniques. The present overview provides a brief and elementary introduction to muscle structure and function and the techniques used to study it. It goes on to give more detailed descriptions of what is known about muscle components and the cross-bridge cycle using structural biology techniques, particularly protein crystallography, electron microscopy and X-ray diffraction. It then has a quick look at muscle mechanics and it summarises what can be learnt about how muscle works based on the other studies covered in the different papers in the special issue. A picture emerges of the main molecular steps involved in the force-producing process; steps that are also likely to be seen in non-muscle myosin interactions with cellular actin filaments. Finally, the remarkable advances made in studying the effects of mutations in the contractile assembly in causing specific muscle diseases, particularly those in heart muscle, are outlined and discussed. View Full-Text
Keywords: myosin filaments; actin filaments; the sarcomere; Z-band; M-band; myosin cross-bridge cycle; hypertrophic cardiomyopathy; dilated cardiomyopathy; rigor muscle; weak-binding state; strong-binding states; sarcomere compliance; myosin filament compliance; actin filament compliance; cross-bridge compliance; time-resolved X-ray diffraction; fluorescence methods; spin probe methods myosin filaments; actin filaments; the sarcomere; Z-band; M-band; myosin cross-bridge cycle; hypertrophic cardiomyopathy; dilated cardiomyopathy; rigor muscle; weak-binding state; strong-binding states; sarcomere compliance; myosin filament compliance; actin filament compliance; cross-bridge compliance; time-resolved X-ray diffraction; fluorescence methods; spin probe methods
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Squire, J. Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview. Int. J. Mol. Sci. 2019, 20, 5715.

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