Cell cycle control of wnt receptor activation

Dev Cell. 2009 Dec;17(6):788-99. doi: 10.1016/j.devcel.2009.11.006.

Abstract

Low-density lipoprotein receptor related proteins 5 and 6 (LRP5/6) are transmembrane receptors that initiate Wnt/beta-catenin signaling. Phosphorylation of PPPSP motifs in the LRP6 cytoplasmic domain is crucial for signal transduction. Using a kinome-wide RNAi screen, we show that PPPSP phosphorylation requires the Drosophila Cyclin-dependent kinase (CDK) L63. L63 and its vertebrate homolog PFTK are regulated by the membrane tethered G2/M Cyclin, Cyclin Y, which mediates binding to and phosphorylation of LRP6. As a consequence, LRP6 phosphorylation and Wnt/beta-catenin signaling are under cell cycle control and peak at G2/M phase; knockdown of the mitotic regulator CDC25/string, which results in G2/M arrest, enhances Wnt signaling in a Cyclin Y-dependent manner. In Xenopus embryos, Cyclin Y is required in vivo for LRP6 phosphorylation, maternal Wnt signaling, and Wnt-dependent anteroposterior embryonic patterning. G2/M priming of LRP6 by a Cyclin/CDK complex introduces an unexpected new layer of regulation of Wnt signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Cycle*
  • Cell Line
  • Cyclins / metabolism
  • Drosophila
  • Humans
  • Low Density Lipoprotein Receptor-Related Protein-6
  • Phosphorylation
  • Proteomics
  • Receptors, LDL / metabolism
  • Wnt Proteins / metabolism*
  • Xenopus laevis

Substances

  • Cyclins
  • LRP6 protein, human
  • Low Density Lipoprotein Receptor-Related Protein-6
  • Receptors, LDL
  • Wnt Proteins