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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Neurabin II mediates doublecortin-dephosphorylation on actin filaments.

Mutations in the human Doublecortin (DCX) gene cause X- linked lissencephaly, a neuronal migration disorder. DCX binds to microtubules and actin filaments. Association of Dcx with F-actin is regulated by site-specific phosphorylation and by neurabin II, an F-actin binding protein that also binds to Dcx. We show here that neurabin II mediates dephosphorylation of Dcx by protein phosphatase 1 (PP1). Furthermore, overexpression of PP1 reduces Dcx phosphorylation and decreases Dcx binding to F-actin. By contrast, abolishing PP1 binding to neurabin II maintains phosphorylation levels of Dcx, leading to a retention of Dcx at F-actin. We suggest that a dynamic regulation of Dcx mediated by neurabin II regulates the translocation of Dcx from F-actin to microtubules and vice versa.[1]

References

  1. Neurabin II mediates doublecortin-dephosphorylation on actin filaments. Tsukada, M., Prokscha, A., Eichele, G. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
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