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J Biol Chem, Vol. 274, Issue 31, 21790-21796, July 30, 1999

Regulation of the Protein Kinase Activity of Shaggy^Zeste-white3 by Components of the Wingless Pathway in Drosophila Cells and Embryos

From the Division of Experimental Therapeutics, Ontario Cancer Institute, and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada

The protein-serine kinase Shaggy^Zeste-white3 (Sgg^Zw3) is the Drosophila homolog of mammalian glycogen synthase kinase-3 and has been genetically implicated in signal transduction pathways necessary for the establishment of patterning. Sgg^Zw3 is a putative component of the Wingless (Wg) pathway, and epistasis analyses suggest that Sgg^Zw3 function is repressed by Wg signaling. Here, we have investigated the biochemical consequences of Wg signaling with respect to the Sgg^Zw3 protein kinase in two types of Drosophila cell lines and in embryos. Our results demonstrate that Sgg^Zw3 activity is inhibited following exposure of cells to Wg protein and by expression of downstream components of Wg signaling, Drosophila frizzled 2 and dishevelled. Wg-dependent inactivation of Sgg^Zw3 is accompanied by serine phosphorylation. We also show that the level of Sgg^Zw3 activity regulates the stability of Armadillo protein and modulates the level of phosphorylation of D-Axin and Armadillo. Together, these results provide direct biochemical evidence in support of the genetic model of Wg signaling and provide a model for dissecting the molecular interactions between the signaling proteins.

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