Dissociation of beta-catenin from Axin and association of beta catenin with phospho-(20 aa) APC in the detruction complex

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

The phosphorylation of the 20 aa repeats in APC results in an increase in affinity for beta-catenin (Ha et al., 2004, Xing et al., 2004; Liu et al., 2006). The binding site of phospho -(20 aa) APC on beta-catenin overlaps the binding site of Axin on beta catenin. In addition, phosphorylated APC prevents the association of Axin with beta-catenin (Ha et al., 2004, Xing et al., 2004). In this model, phosphorylated APC may compete with Axin for beta-catenin binding, resulting in dissociation of the Axin:beta-catenin interaction in the destruction complex (see Kimelman and Xu 2006).

Literature References
PubMed ID Title Journal Year
15327769 Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function

Kimelman, D, Stenkamp, R, Hinds, TR, Xing, Y, Clements, WK, Le Trong, I, Xu, W

Mol Cell 2004
Orthologous Events
Cite Us!