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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Identification of the Axin and Frat binding region of glycogen synthase kinase-3.

Glycogen synthase kinase-3 (GSK-3) is a key component of several signaling pathways including those regulated by Wnt and insulin ligands. Specificity in GSK-3 signaling is thought to involve interactions with scaffold proteins that localize GSK-3 regulators and substrates. This report shows that GSK-3 forms a low affinity homodimer that is disrupted by binding to Axin and Frat. Based on the crystal structure of GSK-3, we have used surface-scanning mutagenesis to identify residues that differentially affect GSK-3 interactions. Mutations that disrupt Frat and Axin cluster at the dimer interface explaining their effect on homodimer formation. Loss of the Axin binding site blocks the ability of dominant negative GSK-3 to cause axis duplication in Xenopus embryos. The Axin binding site is conserved within all GSK-3 proteins, and its loss affects both cell motility and gene expression in the nonmetazoan, Dictyostelium. Surprisingly, we find no genetic interaction between a non-Axin-binding GSK-3 mutant and T-cell factor activity, arguing that Axin interactions alone cannot explain the regulation of T-cell factor-mediated gene expression.[1]

References

  1. Identification of the Axin and Frat binding region of glycogen synthase kinase-3. Fraser, E., Young, N., Dajani, R., Franca-Koh, J., Ryves, J., Williams, R.S., Yeo, M., Webster, M.T., Richardson, C., Smalley, M.J., Pearl, L.H., Harwood, A., Dale, T.C. J. Biol. Chem. (2002) [Pubmed]
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