The F-box protein Slmb restricts the activity of aPKC to polarize epithelial cells

Lara C. Skwarek, Sarah L. Windler, Geert de Vreede, Gregory C. Rogers, David Bilder

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

The Par-3/Par-6/aPKC complex is the primary determinant of apical polarity in epithelia across animal species, but how the activity of this complex is restricted to allow polarization of the basolateral domain is less well understood. In Drosophila, several multiprotein modules antagonize the Par complex through a variety of means. Here we identify a new mechanism involving regulated protein degradation. Strong mutations insupernumerary limbs(slmb), which encodes the substrate adaptor of an SCF-class E3 ubiquitin ligase, cause dramatic loss of polarity in imaginal discs accompanied by tumorous proliferation defects. Slmb function is required to restrain apical aPKC activity in a manner that is independent of endolysosomal trafficking and parallel to the Scribble module of junctional scaffolding proteins. The involvement of the Slmb E3 ligase in epithelial polarity, specifically limiting Par complex activity to distinguish the basolateral domain, points to parallels with polarization of theC. eleganszygote.

Original languageEnglish (US)
Pages (from-to)2978-2983
Number of pages6
JournalDevelopment
Volume141
Issue number15
DOIs
Publication statusPublished - 2014

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Keywords

  • Drosophila
  • Epithelia
  • Par
  • Polarity
  • Tumor
  • Ubiquitin ligase

ASJC Scopus subject areas

  • Developmental Biology
  • Molecular Biology

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