Cloning, Characterization, and Promoter Analysis of Mouse Myo10 Gene

  title={Cloning, Characterization, and Promoter Analysis of Mouse Myo10 Gene},
  author={Mingming Lai and Lin Li and Xingda Ju and Hua-Li Yu and Xiaojuan Zhu},
  journal={Nucleosides, Nucleotides \& Nucleic Acids},
  pages={354 - 365}
Myosin X (Myo10) is an unconventional myosin associated with filopodia motility. Recent studies show that in addition to full-length Myo10, brain expresses a shorter form of Myo10 that lacks a myosin motor domain named headless Myo10. Herein, we analyzed and cloned 2-kb of the 5′-upstream sequences of mouse full-length Myo10 (fMyo10) and headless Myo10 (hMyo10) to understand the transcriptional regulation of the Myo10 gene. The putative transcription factor binding sites and CpG island were… 
1 Citations

Filopodia powered by class x myosin promote fusion of mammalian myoblasts

It is demonstrated that Myo10-driven filopodia facilitate multi-nucleated mammalian muscle formation, and the muscle fusion proteins Myomaker and Myomixer are detected in myoblast filopODia.



Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons

It is reported here that, in addition to full-length Myo10, brain expresses a shorter form of MyO10 that lacks a myosin head domain, which is unable to function as a molecular motor and, like it, contains three pleckstrin homology (PH) domains.

PtdIns (3,4,5) P3 Recruitment of Myo10 Is Essential for Axon Development

Mechanism studies demonstrated that the recruitment of Myo10 through its PH domain to phosphatidylinositol (3,4,5)-trisphosphate (PtdIns) P3 was essential for axon formation and in vivo studies confirmed that Myo 10 was required for neuronal morphological transition during radial neuronal migration in the developmental neocortex.

Headless Myo10 Is a Negative Regulator of Full-length Myo10 and Inhibits Axon Outgrowth in Cortical Neurons*

This study establishes opposing roles for headless and full-length Myo10 in axon outgrowth and reports the first isoform-specific localization of Myosin that localizes to and induces filopodia, structures that are critical for growing axons.

Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin.

The full-length cDNA sequences of human and bovine myosin-X are reported as well as the first characterization of this protein's distribution and biochemical properties, suggesting that this novel unconventionalMyosin plays a role in regions of dynamic actin.

Myosin X regulates netrin receptors and functions in axonal path-finding

A novel role for Myo X is identified in regulating netrin-1 function, which interacts with the netrin receptor deleted in colorectal cancer (DCC) and neogenin, a DCC-related protein.

Myosin rod protein: a novel thick filament component of Drosophila muscle.

Data indicate that MRP is a novel contractile protein that co-integrates with myosin into the thick filament, thereby changing structure and function of the sarcomere.

Myosin-X provides a motor-based link between integrins and the cytoskeleton

Results indicate that Myo10-mediated relocalization of integrins might serve to form adhesive structures and thereby promote filopodial extension.

Myosin X transports Mena/VASP to the tip of filopodia.

  • H. TokuoM. Ikebe
  • Biology
    Biochemical and biophysical research communications
  • 2004

Single-molecule stepping and structural dynamics of myosin X

The motility of dimerized myosin X is studied using the single-molecule fluorescence techniques polTIRF, FIONA and Parallax to measure the rotation angles and three-dimensional position of the molecule during its walk.