Toggling a conformational switch in Wnt/β-catenin signaling: regulation of Axin phosphorylation. The phosphorylation state of Axin controls its scaffold function in two Wnt pathway protein complexes.

Tacchelly-Benites O, Wang Z, Yang E, Lee E, Ahmed Y
Bioessays. 2013 35 (12): 1063-70

PMID: 24105937 · PMCID: PMC3878292 · DOI:10.1002/bies.201300101

The precise orchestration of two opposing protein complexes - one in the cytoplasm (β-catenin destruction complex) and the other at the plasma membrane (LRP6 signaling complex) - is critical for controlling levels of the transcriptional co-factor β-catenin, and subsequent activation of the Wnt/β-catenin signal transduction pathway. The Wnt pathway component Axin acts as an essential scaffold for the assembly of both complexes. How the β-catenin destruction and LRP6 signaling complexes are modulated following Wnt stimulation remains controversial. A recent study in Science by He and coworkers reveals an underlying logic for Wnt pathway control in which Axin phosphorylation toggles a switch between the active and inactive states. This mini-review focuses on this and two other recent studies that provide insight into the initial signaling events triggered by Wnt exposure. We emphasize regulation of the β-catenin destruction and LRP6 signaling complexes and propose a framework for future work in this area.

© 2013 WILEY Periodicals, Inc.

MeSH Terms (8)

Animals Axin Protein beta Catenin Humans Phosphorylation Protein Binding Signal Transduction Wnt Signaling Pathway

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