Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 276, Issue 3, Pages 1162-1169Publisher
ACADEMIC PRESS INC
DOI: 10.1006/bbrc.2000.3607
Keywords
disheveled; Axin; beta-catenin; protein interaction; Wnt
Categories
Funding
- NCI NIH HHS [R01CA75353] Funding Source: Medline
- NIGMS NIH HHS [5 RO1 GM56934] Funding Source: Medline
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Disheveled blocks the degradation of beta-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 murine 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) mere identified that can promote the association of Axin and Disheveled. We found that the DM 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 beta-catenin whereas the PDZ domain was not essential to this function. (C) 2000 Academic Press.
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