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

@article{Sousa2006Myo10IB,
  title={Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons},
  author={Aurea D Sousa and Jonathan S. Berg and Brian William Robertson and Rick B. Meeker and Richard E. Cheney},
  journal={Journal of Cell Science},
  year={2006},
  volume={119},
  pages={184 - 194}
}
Although Myo10 (myosin-X) is an unconventional myosin associated with filopodia, little is known about its isoforms and roles in the nervous system. We report here that, in addition to full-length Myo10, brain expresses a shorter form of Myo10 that lacks a myosin head domain. This `headless' Myo10 is thus unable to function as a molecular motor, but is otherwise identical to full-length Myo10 and, like it, contains three pleckstrin homology (PH) domains, a myosin-tail homology 4 (MyTH4) domain… 

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References

SHOWING 1-10 OF 51 REFERENCES

Myr 8, A Novel Unconventional Myosin Expressed during Brain Development Associates with the Protein Phosphatase Catalytic Subunits 1α and 1γ1

TLDR
The structural features and restricted expression patterns suggest that members of this novel class of unconventional myosins comprise a mechanism to target selectively the protein phosphatase 1 catalytic subunits 1α and/or 1γ in developing brain.

Myr 8, a novel unconventional myosin expressed during brain development associates with the protein phosphatase catalytic subunits 1alpha and 1gamma1.

TLDR
The structural features and restricted expression patterns suggest that members of this novel class of unconventional myosins comprise a mechanism to target selectively the protein phosphatase 1 catalytic subunits 1alpha and/or 1gamma in developing brain.

Myosin function in nervous and sensory systems.

TLDR
The roles that neuronal myosins play in a wide variety of cellular functions in the developing nervous system, including neuronal migration, process outgrowth, and growth cone motility, as well as other aspects of morphogenesis, axonal transport, and synaptic and sensory functions are reviewed.

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

TLDR
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: a molecular motor at the cell's fingertips.

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

TLDR
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

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

Myosin-X is an unconventional myosin that undergoes intrafilopodial motility

TLDR
The localization and movements of M10 strongly suggest that it functions as a motor for intrafilopodial motility, which is reported here that myosin-X (Myo10 or M10), the founding member of a novel class of myosins, localizes to the tips of filopodia and undergoes striking forward and rearward movements within filopode motility.

Motor Function and Regulation of Myosin X*

TLDR
The results suggest that myosin X is a nonprocessive motor, and ADP did not significantly inhibit the actin-activated ATPase activity of myOSin X, suggesting that the ADP release step is not rate-limiting.
...