Journal
GENES & DEVELOPMENT
Volume 17, Issue 22, Pages 2753-2764Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1142603
Keywords
Wnt; beta-catenin; axin; adenomatous polyposis coli (APQ); crystal structure
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Funding
- NCI NIH HHS [R01 CA090351, CA90351] Funding Source: Medline
- NICHD NIH HHS [HD27262, R01 HD027262] Funding Source: Medline
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The beta-catenin destruction complex is central to canonical Wnt/beta-catenin signaling. The scaffolding protein Axin and the tumor suppressor adenomatous polyposis coli protein (APC) are critical components of this complex, required for rapid beta-catenin turnover. We determined the crystal structure of a complex between beta-catenin and the beta-catenin-binding domain of Axin (Axin-CBD). The Axin-CBD forms a helix that occupies the groove formed by the third and fourth armadillo repeats of beta-catenin and thus precludes the simultaneous binding of other beta-catenin partners in this region. Our biochemical studies demonstrate that, when phosphorylated, the 20-amino acid repeat region of APC competes with Axin for binding to beta-catenin. We propose that a key function of APC in the beta-catenin destruction complex is to remove phosphorylated beta-catenin product from the active site.
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