2. Academic Validation
  3. WDR26 is a new partner of Axin1 in the canonical Wnt signaling pathway

WDR26 is a new partner of Axin1 in the canonical Wnt signaling pathway

  • FEBS Lett. 2016 May;590(9):1291-303. doi: 10.1002/1873-3468.12180.
Toshiyasu Goto 1,  Junhei Matsuzawa 1,  Shun-Ichiro Iemura 2,  Tohru Natsume 2,  Hiroshi Shibuya 1
Affiliations

Affiliations

  • 1 Department of Molecular Cell Biology, Medical Research Institute, Tokyo Medical and Dental University, Japan.
  • 2 Molecular Profiling Research Center for Drug Discovery, National Institutes of Advanced Industrial Science and Technology, Tokyo, Japan.
PMID: 27098453 DOI: 10.1002/1873-3468.12180
Abstract

The stability of β-catenin is very important for canonical Wnt signaling. A protein complex including Axin/APC/GSK3β phosphorylates β-catenin to be degraded by ubiquitination with β-TrCP. In the recent study, we isolated WDR26, a protein that binds to Axin. Here, we found that WDR26 is a negative regulator of the canonical Wnt signaling pathway, and that WDR26 affected β-catenin levels. In addition, WDR26/Axin binding is involved in the ubiquitination of β-catenin. These results suggest that WDR26 plays a negative role in β-catenin degradation in the Wnt signaling pathway.

Keywords

Axin1; WDR26; Wnt; ubiquitination; β-catenin.

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