Journal
JOURNAL OF CELL SCIENCE
Volume 124, Issue 22, Pages 3733-3741Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.023549
Keywords
Myosin-X; Myo10; Filopodia; MyTH4-FERM; Intrafilopodial motility
Categories
Funding
- National Institutes of Heath, National Institute on Deafness and Other Communication Disorders [R01-DC03299]
- National Institutes of Heath, National Heart, Lung, and Blood Institute [P01-HL080166]
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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.
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