Key result
Mammalian myosin 5a and Drosophila myosin 7a both have a folded inactive state, but the structural details of their regulation differ greatly.
This review highlights the distinct structural mechanisms regulating mammalian myosin 5a and Drosophila myosin 7a despite both having a folded inactive state.
Species-specific myosin regulation urges caution in model translation; leaves open conserved cardiac targets for future study.
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.
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Siththanandan et al. (2011) reported a review. Mammalian myosin 5a and Drosophila myosin 7a both have a folded inactive state, but the structural details of their regulation differ greatly.
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