Regulation of the protein kinase activity of Shaggy(Zeste-white3) by components of the wingless pathway in Drosophila cells and embryos

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 1999-07, Vol.274 (31), p.21790-21796
Main Authors: Ruel, L, Stambolic, V, Ali, A, Manoukian, A S, Woodgett, J R
Format: Article
Language:English
Subjects:
Animals
Cell Line
Drosophila melanogaster - embryology
Drosophila melanogaster - genetics
Drosophila melanogaster - physiology
Drosophila Proteins
Embryo, Nonmammalian - physiology
Gene Expression Regulation, Enzymologic
Glycogen Synthase Kinase 3
Metallothionein - genetics
Promoter Regions, Genetic
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Proto-Oncogene Proteins - metabolism
Recombinant Proteins - metabolism
Repressor Proteins - metabolism
Signal Transduction
Transfection
Wnt1 Protein
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Summary: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.
ISSN:1083-351X
DOI:10.1074/jbc.274.31.21790