aPKC phosphorylation of Bazooka defines the apical/lateral border in Drosophila epithelial cells

Cell. 2010 Apr 30;141(3):509-23. doi: 10.1016/j.cell.2010.02.040.

Abstract

Bazooka (PAR-3), PAR-6, and aPKC form a complex that plays a key role in the polarization of many cell types. In epithelial cells, however, Bazooka localizes below PAR-6 and aPKC at the apical/lateral junction. Here, we show that Baz is excluded from the apical aPKC domain in epithelia by aPKC phosphorylation, which disrupts the Baz/aPKC interaction. Removal of Baz from the complex is epithelial-specific because it also requires the Crumbs complex, which prevents the Baz/PAR-6 interaction. In the absence of Crumbs or aPKC phosphorylation of Baz, mislocalized Baz recruits adherens junction components apically, leading to a loss of the apical domain and an expansion of lateral. Thus, apical exclusion of Baz by Crumbs and aPKC defines the apical/lateral border. Although Baz acts as an aPKC targeting and specificity factor in nonepithelial cells, our results reveal that it performs a complementary function in positioning the adherens junction in epithelia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Genetically Modified
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / cytology
  • Drosophila melanogaster / metabolism*
  • Embryo, Nonmammalian / metabolism
  • Epithelial Cells / metabolism*
  • Female
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Ovarian Follicle / metabolism
  • Ovary / cytology
  • Ovary / metabolism
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Protein Structure, Tertiary

Substances

  • Drosophila Proteins
  • Intracellular Signaling Peptides and Proteins
  • baz protein, Drosophila
  • PKC-3 protein
  • Par-6 protein, Drosophila
  • Protein Kinase C