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Traffic. 2016 Aug;17(8):839-59. doi: 10.1111/tra.12388. Epub 2016 Mar 31.

Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.

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Laboratory of Molecular Physiology, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, B50/3523, Bethesda, MD 20892-8015, USA.


Members of the myosin superfamily are involved in all aspects of eukaryotic life. Their function ranges from the transport of organelles and cargos to the generation of membrane tension, and the contraction of muscle. The diversity of physiological functions is remarkable, given that all enzymatically active myosins follow a conserved mechanoenzymatic cycle in which the hydrolysis of ATP to ADP and inorganic phosphate is coupled to either actin-based transport or tethering of actin to defined cellular compartments. Kinetic capacities and limitations of a myosin are determined by the extent to which actin can accelerate the hydrolysis of ATP and the release of the hydrolysis products and are indispensably linked to its physiological tasks. This review focuses on kinetic competencies that - together with structural adaptations - result in myosins with unique mechanoenzymatic properties targeted to their diverse cellular functions.


actin; allostery; cation; cytoskeleton; mechanoenzymology; molecular motor; muscle; myosin; transporter

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