DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila
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. In this work 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.
- Authors:
-
- Consejo Superior de Investigaciones Científicas, Madrid (Spain). Centro de Biología Molecular Severo Ochoa; Universidad Autonóma de Madrid, Cantoblanco, Madrid (Spain)
- Publication Date:
- Research Org.:
- Consejo Superior de Investigaciones Cientificas (CSIC), Madrid (Spain); Universidad Autonóma de Madrid, Cantoblanco, Madrid (Spain)
- Sponsoring Org.:
- Comunidad Autónoma de Madrid (CAM); Dirección General de Investigación Científica y Técnica; Fundación Ramón Areces
- OSTI Identifier:
- 1625133
- Grant/Contract Number:
- 08.5/0030/2000; PB98-0682; BMC2002-00411; SAF1999-0053; 2FD97-1429; SAF2000-0175; 08.1/0060/2000
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Cell Biology
- Additional Journal Information:
- Journal Volume: 166; Journal Issue: 4; Journal ID: ISSN 0021-9525
- Publisher:
- Rockefeller University Press
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; cell biology; DaPKC; Crumbs; Drosophila; epithelial cell polarity; signal transduction
Citation Formats
Sotillos, Sol, Díaz-Meco, María Teresa, Caminero, Eva, Moscat, Jorge, and Campuzano, Sonsoles. DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila. United States: N. p., 2004.
Web. doi:10.1083/jcb.200311031.
Sotillos, Sol, Díaz-Meco, María Teresa, Caminero, Eva, Moscat, Jorge, & Campuzano, Sonsoles. DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila. United States. https://doi.org/10.1083/jcb.200311031
Sotillos, Sol, Díaz-Meco, María Teresa, Caminero, Eva, Moscat, Jorge, and Campuzano, Sonsoles. Mon .
"DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila". United States. https://doi.org/10.1083/jcb.200311031. https://www.osti.gov/servlets/purl/1625133.
@article{osti_1625133,
title = {DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila},
author = {Sotillos, Sol and Díaz-Meco, María Teresa and Caminero, Eva and Moscat, Jorge and Campuzano, Sonsoles},
abstractNote = {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. In this work 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.},
doi = {10.1083/jcb.200311031},
journal = {Journal of Cell Biology},
number = 4,
volume = 166,
place = {United States},
year = {Mon Aug 09 00:00:00 EDT 2004},
month = {Mon Aug 09 00:00:00 EDT 2004}
}
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Casein kinase 1 family proteins promote Slimb-dependent Expanded degradation.
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The Scribble Cell Polarity Module in the Regulation of Cell Signaling in Tissue Development and Tumorigenesis
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