Abstract：
: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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Kerber ML,Cheney REdoi
10.1242/jcs.023549subject
Has Abstractpub_date
2011-11-15 00:00:00pages
3733-41issue
Pt 22eissn
0021-9533issn
1477-9137pii
124/22/3733journal_volume
124pub_type
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pub_type： 杂志文章
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