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PMID:15302858
| Citation |
Sotillos, S, Díaz-Meco, MT, Caminero, E, Moscat, J and Campuzano, S (2004) DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila. J. Cell Biol. 166:549-57 |
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| 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. |
| Links |
PubMed PMC2172211 Online version:10.1083/jcb.200311031 |
| Keywords |
Amino Acid Sequence; Animals; Body Patterning; Cell Polarity; DNA, Complementary/metabolism; Drosophila; Drosophila Proteins/metabolism; Epithelial Cells/cytology; Gene Expression Regulation, Developmental; Gene Library; Genes, Dominant; Glutathione Transferase/metabolism; Immunohistochemistry; Membrane Proteins/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phosphorylation; Protein Binding; Protein Kinase C/metabolism; Protein Processing, Post-Translational; Recombinant Fusion Proteins/metabolism; Tight Junctions; Wing/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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See also
References
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