Cyclin-dependent kinase 2 regulates the interaction of Axin with beta-catenin |
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Authors: | Kim Sung Il Park Chun Shik Lee Mi Su Kwon Min Seong Jho Eek-hoon Song Woo Keun |
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Affiliation: | Department of Life Science, Kwangju Institute of Science and Technology, Kwangju 500-712, Republic of Korea. |
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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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Keywords: | Axin Cyclin-dependent kinase 2 Phosphorylation β-Catenin |
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