Like GLI3, GLI2 has putative GSK3 sites that contribute to the proteasome-dependent degradation of the protein in the absence of Hh signal. Deletion of the GSK3 phosphorylation sites abrogates the interaction with beta-TrCP, stabilizes GLI2 protein and increases the expression of a GLI-dependent reporter, consistent with a role for GSK3 in promoting GLI2 degradation (Pan et al, 2006).
Pan, Y, Bai, CB, Wang, B, Joyner, AL
protein serine/threonine kinase activity of GSK3B [cytosol]
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