Cyclin-dependent kinase 2 regulates the interaction of Axin with β-catenin

Sung Il Kim, Chun Shik Park, Mi Su Lee, Min Seong Kwon, Eek Hoon Jho, Woo Keun Song

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Axin, a negative regulator of Wnt, forms a complex with glycogen synthase kinase 3β, β-catenin, and adenomatous polyposis coli and promotes GSK3β-dependent phosphorylation of β-catenin, thereby stimulating degradation of the β-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 β-catenin. This suggests that cyclin A/CDK2 is a negative regulator of β-catenin-mediated signal transduction, which exerts its effects through phosphorylation of Axin.

Original languageEnglish
Pages (from-to)478-483
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - 30 Apr 2004


  • Axin
  • Cyclin-dependent kinase 2
  • Phosphorylation
  • β-Catenin


Dive into the research topics of 'Cyclin-dependent kinase 2 regulates the interaction of Axin with β-catenin'. Together they form a unique fingerprint.

Cite this