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Myosin: Cellular Molecular Motor

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Cellular Nanomachines

Abstract

Myosins are a superfamily of ATP-dependent, actin-based motor proteins. In addition to muscle contraction, myosins are involved in a wide range of motility functions in cells, including transport of intracellular cargo. Typically, myosin molecules are composed of a heavy chain having a tail, hinge, and head domain and light chain present near the myosin head that modulates calcium-dependent transduction of force by myosin. The myosin head has both actin binding and ATP binding and ATPase activity. In resting state, myosin is bound to actin. When ATP binds to the myosin head, the head dissociates from the actin filament. Hydrolysis of bound ATP to ADP and the release of phosphate establish the rigor state of myosin (reestablishes myosin–actin interaction), generating force in the process to walk along the actin filament. Binding of a new ATP molecule to the myosin head releases myosin from actin to repeat the cycle. The structure and function of myosin are globally conserved.

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  1. Department of Physiology, Wayne State University School of Medicine, Detroit, MI, USA

    Bhanu P. Jena

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Jena, B.P. (2020). Myosin: Cellular Molecular Motor. In: Cellular Nanomachines. Springer, Cham. https://doi.org/10.1007/978-3-030-44496-9_7

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