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Reference Report
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| Citation | Sotillos, S., Diaz-Meco, M.T., Caminero, E., Moscat, J., Campuzano, S. (2004). DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila. J. Cell Biol. 166(4): 549--557. (Export to RIS) | ||
| FlyBase ID | FBrf0180375 | ||
| Publication Type | Research paper | ||
| PubMed ID | 15302858 | ||
| PubMed Abstract | Both in Drosophila and vertebrate epithelial cells, the establishment of apicobasal polarity requires the apically localized, membrane-associated Par-3-Par-6-aPKC protein complex. In Drosophila, this complex colocalizes with the Crumbs-Stardust (Sdt)-Pals1-associated TJ protein (Patj) complex. Genetic and molecular analyses suggest a functional relationship between them. We show, by overexpression of a kinase-dead Drosophila atypical PKC (DaPKC), the requirement for the kinase activity of DaPKC to maintain the position of apical determinants and to restrict the localization of basolateral ones. We demonstrate a novel physical interaction between the apical complexes, via direct binding of DaPKC to both Crb and Patj, and identify Crumbs as a phosphorylation target of DaPKC. This phosphorylation of Crumbs is functionally significant. Thus, a nonphosphorylatable Crumbs protein behaves in vivo as a dominant negative. Moreover, the phenotypic effect of overexpressing wild-type Crumbs is suppressed by reducing DaPKC activity. These results provide a mechanistic framework for the functional interaction between the Par-3-Par-6-aPKC and Crumbs-Sdt-Patj complexes based in the posttranslational modification of Crb by DaPKC. | ||
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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | J. Cell Biol. | ||
| Title | Journal of Cell Biology | ||
| Publication Year | 1966- | ||
| ISBN/ISSN | 0021-9525 | ||
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Data from Reference
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| Alleles (10)
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| Constructs (8)
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| Genes (10)
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| Natural transposons (1)
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