title: Regulation of myosin 5a and myosin 7a.
abstract: 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.
authors.affiliation: Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
authors.forename: Verl B
authors.initials: VB
authors.lastname: Siththanandan
authors.forename: James R
authors.initials: JR
authors.lastname: Sellers
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D006801:Humans; D020460:Melanosomes / Q000378:metabolism; D008958:Models, Molecular; D024701:Myosin Type V / Q000378:metabolism* / Q000648:ultrastructure; D000081412:Myosin VIIa; D009218:Myosins / Q000378:metabolism* / Q000648:ultrastructure; D011487:Protein Conformation; D020033:Protein Isoforms / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D000199:Actins; C000631455:MYO7A protein, human; D000081412:Myosin VIIa; D020033:Protein Isoforms; C000631458:myosin 7a, Drosophila; D024701:Myosin Type V; D009218:Myosins