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Title

DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila

AuthorsSotillos, Sol ; Díaz-Meco, María T.; Caminero, Eva ; Moscat, Jorge ; Campuzano, Sonsoles
KeywordsDaPKC
Crumbs
Drosophila
Epithelial cell polarity
Signal transduction
Issue Date9-Aug-2004
PublisherRockefeller University Press
CitationJCB, Volume 166, Number 4, 549-557
AbstractBoth 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
Publisher version (URL)http://dx.doi.org/10.1083/jcb.200311031
URIhttp://hdl.handle.net/10261/7902
DOI10.1083/jcb.200311031
ISSN0021-9525
E-ISSN1540-8140
Appears in Collections:(CBM) Artículos
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