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

  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},
  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… 

Figures from this paper

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 and its motorless isoform differentially modulate dendritic spine development by regulating trafficking and retention of vasodilator-stimulated phosphoprotein

This study demonstrates a novel biological function for Hdl-Myo10 and an important new role for both Myo10 isoforms in the development of dendritic spines and synapses in hippocampal neurons.

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.

Expression of unconventional myosin genes during neuronal development in zebrafish.

Myosin-X: a MyTH-FERM myosin at the tips of filopodia

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.

Myosin X.

  • H. Tokuo
  • Biology
    Advances in experimental medicine and biology
  • 2020
This chapter addresses the structure of the Myo10 gene; the molecular structure of Myosin X protein with its multiple domains; the regulation of actin structures induced in cells by Myo 10; the expression and function of Myo12 in vitro and in vivo; and the role of MyO10 in cancer.

Myosin16b: The COOH-tail region directs localization to the nucleus and overexpression delays S-phase progression.

It is found that Myo16b displays predominant localization in the nucleus of cells transitioning through interphase, but is not associated with processes of mitosis.

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.

Headless Myo10 is a regulator of microtubule stability during neuronal development

In vivo studies reveal that hMyo10‐mediated microtubule stability has a profound effect on both neuronal migration and dendritic arborization in the mammalian cerebral cortex, suggesting that h myosin X is involved in neuronal development both in vitro and in vivo by regulating micro Tubule stability.

Myosin-X is a molecular motor that functions in filopodia formation

It is shown that siRNA-mediated knockdown of Myo10 in HeLa cells leads to a dramatic loss of dorsal filopodia, and additional experiments indicate that it acts downstream of Cdc42 and can promote filopadia in the absence of VASP proteins.



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

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.

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.

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.

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.

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 is an unconventional myosin that undergoes intrafilopodial motility

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*

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.