Domains of Axin and Disheveled required for interaction and function in Wnt signaling

M. A. Julius, B. Schelbert, W. Hsu, E. Fitzpatrick, E. Jho, F. Fagotto, F. Costantini, J. Kitajewski

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


Disheveled blocks the degradation of β-catenin in response to Wnt signal by interacting with the scaffolding protein, Axin. To define this interaction in detail we undertook a mutational and binding analysis of the routine Axin and Disheveled proteins. The DIX domain of Axin was found to be important for association with Disheveled and two other regions of Axin (between residues 1-168 and 600-810) were identified that can promote the association of Axin and Disheveled. We found that the DIX domain of Disheveled is critical for association with Axin in vivo and for Disheveled activity. The Disheveled DIX domain controlled the ability of Disheveled to induce the accumulation of cytosolic β-catenin whereas the PDZ domain was not essential to this function. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1162-1169
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 5 Oct 2000


  • Axin
  • Disheveled
  • Protein interaction
  • Wnt
  • β-catenin


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