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Myosin-X: a MyTH-FERM myosin at the tips of filopodia
Michael L. Kerber, Richard E. Cheney


Myosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia. Although the head domain of Myo10 enables it to function as an actin-based motor, its tail contains binding sites for several molecules with central roles in cell biology, including phosphatidylinositol (3,4,5)-trisphosphate, microtubules and integrins. Myo10 also undergoes fascinating long-range movements within filopodia, which appear to represent a newly recognized system of transport. Myo10 is also unusual in that it is a myosin with important roles in the spindle, a microtubule-based structure. Exciting new studies have begun to reveal the structure and single-molecule properties of this intriguing myosin, as well as its mechanisms of regulation and induction of filopodia. At the cellular and organismal level, growing evidence demonstrates that Myo10 has crucial functions in numerous processes ranging from invadopodia formation to cell migration.


  • Note added in proof

    The structure of the PH1–PH2 region has recently been reported, and this region forms a rigid supramodule whose lipid-binding pockets are positioned side-by-side, allowing Myo10 to bind to phosphatidylinositol (3,4,5)-trisphosphate with high specificity and avidity (Lu et al., 2011).

  • Funding

    Our work is supported by grants from the National Institutes of Heath, National Institute on Deafness and Other Communication Disorders [grant number R01-DC03299 to R.E.C.]; and National Institutes of Heath, National Heart, Lung, and Blood Institute [grant number P01-HL080166 to R.E.C.]. Deposited in PMC for release after 12 months.

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