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  • Title: Cyclin-dependent kinase 2 regulates the interaction of Axin with beta-catenin.
    Author: Kim SI, Park CS, Lee MS, Kwon MS, Jho EH, Song WK.
    Journal: Biochem Biophys Res Commun; 2004 Apr 30; 317(2):478-83. PubMed ID: 15063782.
    Abstract:
    Axin, a negative regulator of Wnt, forms a complex with glycogen synthase kinase 3beta, beta-catenin, and adenomatous polyposis coli and promotes GSK3beta-dependent phosphorylation of beta-catenin, thereby stimulating degradation of the beta-catenin. An essential step in that process is the phosphorylation of Axin. Examination of Axin's amino acid sequence revealed it to contain six arginine-X-leucine (RXL) sequences, the cyclin-dependent kinase 2 (CDK2) binding motif, and 10 CDK2 consensus phosphorylation sequences. We also found that cyclin A/CDK2 phosphorylates Axin, thereby enhancing its association with beta-catenin. This suggests that cyclin A/CDK2 is a negative regulator of beta-catenin-mediated signal transduction, which exerts its effects through phosphorylation of Axin.
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