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.

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.
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DOI:
10.1002/bies.201300101
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发表时间:
2013-12
期刊:
影响因子:
4
通讯作者:
Ahmed, Yashi
Ahmed, Yashi
中科院分区:
生物学3区
文献类型:
--
作者:
Tacchelly-Benites, Ofelia;Wang, Zhenghan;Yang, Eungi;Lee, Ethan;Ahmed, Yashi

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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 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 colleagues 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.
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