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  Doublecortin association with actin filaments is regulated by neurabin II.

Tsukada, M., Prokscha, A., Ungewickel, E., & Eichele, G. (2005). Doublecortin association with actin filaments is regulated by neurabin II. Journal of Biological Chemistry, 280(12), 11361-11368. doi:10.1074/jbc.M405525200.

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Tsukada, M., Author
Prokscha, A., Author
Ungewickel, E., Author
Eichele, G.1, Author              
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1Department of Molecular Embryology, Max Planck Institute for Experimental Endocrinology, Max Planck Society, ou_1565140              

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 Abstract: Mutations in the human Doublecortin (DCX) gene cause X-linked lissencephaly, a neuronal migration disorder affecting the neocortex and characterized by mental retardation and epilepsy. Because dynamic cellular asymmetries such as those seen in cell migration critically depend on a cooperation between the microtubule and actin cytoskeletal filament systems, we investigated whether Dcx, a microtubule-associated protein, is engaged in cytoskeletal cross-talk. We now demonstrate that Dcx co-sediments with actin filaments (F-actin), and using light and electron microscopy and spin down assays, we show that Dcx induces bundling and cross-linking of microtubules and F-actin in vitro. It has recently been shown that binding of Dcx to microtubules is negatively regulated by phosphorylation of the Dcx at Ser-47 or Ser-297. Although the phosphomimetic green fluorescent protein (GFP)-Dcx(S47E) transfected into COS-7 cells had a reduced affinity for microtubules, we found that pseudophosphorylation was not sufficient to cause Dcx to bind to F-actin. When cells were co-transfected with neurabin II, a protein that binds F-actin as well as Dcx, GFP-Dcx and to an even greater extent GFP-Dcx(S47E) became predominantly associated with filamentous actin. Thus Dcx phosphorylation and neurabin II combinatorially enhance Dcx binding to F-actin. Our findings raise the possibility that Dcx acts as a molecular link between microtubule and actin cytoskeletal filaments that is regulated by phosphorylation and neurabin II.

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Language(s): eng - English
 Dates: 2005-03-25
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M405525200
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 280 (12) Sequence Number: - Start / End Page: 11361 - 11368 Identifier: -