A Cul-3-BTB ubiquitylation pathway regulates junctional levels and asymmetry of core planar polarity proteins

• DOI: 10.1242/dev.089656
• Publication Date: 2013-03-14T03:11:30Z
• Authors: Helen Strutt; Elizabeth Searle; Victoria Thomas-M...; Rosalind Brookfield; David Strutt
• Keywords: Dishevelled; Polarity (international relations)

The asymmetric localisation of core planar polarity proteins at apicolateral junctions is required to specify cell in the plane epithelia. This distribution proposed require amplification an initial asymmetry by feedback loops. In addition, generation appears regulation protein levels, but importance such and underlying mechanisms unknown. Here we show that ubiquitylation acts through more than one mechanism control levels Drosophila, without this cellular compromised. Levels Dishevelled are regulated a Cullin-3-Diablo/Kelch ubiquitin ligase complex, activity which most likely controlled neddylation. Furthermore, deubiquitylating enzyme Fat facets maintain Flamingo junctions. Notably, does not alter total or Flamingo, only junctional population. When either increased decreased disruption machinery, their reduced leads tissue level. Loss altered can be explained reference models for asymmetry.