Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10956936 | Molecular and Cellular Neuroscience | 2005 | 12 Pages |
Abstract
Doublecortin (DCX) is a microtubule-associated protein involved in neuronal migration, which causes X-linked lissencephaly and subcortical laminar heterotopia (SCLH) when mutated. Here we show that DCX interacts with the ubiquitin-specific protease Drosophila fat facets related on X chromosome (DFFRX). This interaction was confirmed by targeted mutagenesis, colocalization, and immunoprecipitation studies. DFFRX is thought to deubiquitinate specific substrates including β-catenin, preventing their degradation by the proteasome. Interestingly, unlike β-catenin, no ubiquitinated forms of DCX could be detected, and indeed we show that DCX interacts with a novel recognition domain in DFFRX, located outside of its catalytic site. We also show that DFFRX associates with microtubules at specific subcellular compartments, including those enriched in DCX. These results thus suggest that in addition to vesicular trafficking, DCX may play a role in the regulation of cell adhesion via its interaction with DFFRX in migrating and differentiating neurons.
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Authors
Gaëlle Friocourt, Caroline Kappeler, Yoann Saillour, Fabien Fauchereau, Manuel S. Rodriguez, Nadia Bahi, Marie-Claude Vinet, Philippe Chafey, Karine Poirier, Shinichiro Taya, Stephen A. Wood, Catherine Dargemont, Fiona Francis, Jamel Chelly,