J Biol Chem 2002 May 03;27718:16147-52. doi: 10.1074/jbc.M112363200.

Glycogen synthase kinase-3 beta mutagenesis identifies a common binding domain for GBP and Axin.

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Glycogen synthase kinase-3 beta (GSK-3) is a key downstream target of Wnt signaling and is regulated by its interactions with activating and inhibitory proteins. We and others have shown that GSK-3 activity toward non-primed substrates is regulated in part through a competition between its activating (Axin) and inhibitory (GBP/FRAT) binding partners. Here we use a reverse two-hybrid screen to identify mutations in GSK-3 that alter binding to GBP and Axin. We find that these mutations overlap and propose that GBP and Axin compete for binding to the same region of GSK-3. We use these mutations to examine the ability of GSK-3 to block eye development in Xenopus embryos and suggest that GSK-3 regulates eye development through a non-Wnt pathway.

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Species referenced: Xenopus
Genes referenced: frat1 gsk3b gys1 pias1