Department of Cell and Molecular Physiology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7545, USA.
J Cell Sci. 2011 Nov 15;124(Pt 22):3733-41. doi: 10.1242/jcs.023549.
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.
肌球蛋白- X（Myo10）是一种具有 MyTH4-FERM 结构域的非传统肌球蛋白，它以其在丝状伪足尖端的显著定位及其诱导丝状伪足的能力而闻名。尽管 Myo10 的头部结构域使其能够作为肌动蛋白依赖的马达发挥作用，但它的尾部包含了几个在细胞生物学中具有核心作用的分子的结合位点，包括磷脂酰肌醇（3,4,5）-三磷酸、微管和整合素。Myo10 还在丝状伪足内进行着引人注目的长程运动，这似乎代表了一种新发现的运输系统。Myo10 还很不寻常，因为它是一种在纺锤体（一种基于微管的结构）中具有重要作用的肌球蛋白。令人兴奋的新研究开始揭示这种有趣的肌球蛋白的结构和单分子特性，以及其调节和诱导丝状伪足的机制。在细胞和生物体水平上，越来越多的证据表明 Myo10 在从侵袭伪足形成到细胞迁移等众多过程中具有至关重要的功能。
