The myosin superfamily is diverse in its structure, kinetic mechanisms and cellular function. The enzymatic activities of most myosins are regulated by some means such as Ca2+ ion binding, phosphorylation or binding of other proteins. In the present review, we discuss the structural basis for the regulation of mammalian myosin 5a and Drosophila myosin 7a. We show that, although both myosins have a folded inactive state in which domains in the myosin tail interact with the motor domain, the details of the regulation of these two myosins differ greatly.
Conference Article| September 21 2011
Regulation of myosin 5a and myosin 7a
Verl B. Siththanandan;
James R. Sellers
James R. Sellers 1
1Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, U.S.A.
1To whom correspondence should be addressed (email email@example.com).
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Verl B. Siththanandan, James R. Sellers; Regulation of myosin 5a and myosin 7a. Biochem Soc Trans 1 October 2011; 39 (5): 1136–1141. doi: https://doi.org/10.1042/BST0391136
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