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J Biol Chem, Vol. 274, Issue 31, 21790-21796, July 30, 1999
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
ShaggyZeste-white3 (SggZw3) 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. SggZw3 is a
putative component of the Wingless (Wg) pathway, and epistasis analyses
suggest that SggZw3 function is repressed by Wg signaling.
Here, we have investigated the biochemical consequences of Wg signaling
with respect to the SggZw3 protein kinase in two types of
Drosophila cell lines and in embryos. Our results
demonstrate that SggZw3 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
SggZw3 is accompanied by serine phosphorylation. We also
show that the level of SggZw3 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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