Abstract
Myosin X (Myo10), an actin-based molecular motor, induces filopodia formation and controls cell migration in vitro. In the 25 years since Myo10 was first identified, it has been implicated in several different functions in different cell types including phagocytosis in macrophages, axon outgrowth in neurons, cell-cell adhesion in epithelial and endothelial cells, podosome formation in osteoclasts, spindle-pole positioning in meiosis and mitosis of cultured cells, migration of melanocytes and cranial neural crest cells, and invadopodia formation in cancer cells. Recently, the availability of Myo10-knockout (Myo10KO) mice has allowed for tremendous progress toward understanding the biological function of Myo10 in vivo.
In this chapter, I address the structure of the Myo10 gene; the molecular structure of Myo10 protein with its multiple domains, e.g., PH, MyTH4, and FERM domains; the regulation of actin structures induced in cells by Myo10; the expression and function of Myo10 in vitro and in vivo; and the role of Myo10 in cancer. Previous reviews on Myo10 include Divito MM, Cheney RE, (Myosins: a superfamily of molecular motors chapter 14 MYOSIN X. In: Proteins and cell regulation, vol 7. Springer, Dordrecht, 2008) and Kerber ML, Cheney RE (J Cell Sci 124:3733–3741).
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Acknowledgements
I am grateful to Lynne M. Coluccio for her helpful comments and suggestions. I apologize for not citing all the relevant references because of space limitation. The work in the author’s laboratory is supported by NIH R01 GM111615 to L.M.C., the Boston University Clinical and Translational Science Institute (1UL1TR001430) and NIH R03 DC009887 to H.T.
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Tokuo, H. (2020). Myosin X. In: Coluccio, L. (eds) Myosins. Advances in Experimental Medicine and Biology, vol 1239. Springer, Cham. https://doi.org/10.1007/978-3-030-38062-5_17
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