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WDR 26 is a new partner of Axin1 in the canonical Wnt signaling pathway
Author(s) -
Goto Toshiyasu,
Matsuzawa Junhei,
Iemura Shunichiro,
Natsume Tohru,
Shibuya Hiroshi
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12180
Subject(s) - wnt signaling pathway , lrp6 , regulator , phosphorylation , lrp5 , catenin , microbiology and biotechnology , signal transduction , chemistry , ubiquitin , beta catenin , biology , biochemistry , gene
The stability of β‐catenin is very important for canonical Wnt signaling. A protein complex including Axin/ APC / GSK 3β phosphorylates β‐catenin to be degraded by ubiquitination with β‐Tr CP . In the recent study, we isolated WDR 26, a protein that binds to Axin. Here, we found that WDR 26 is a negative regulator of the canonical Wnt signaling pathway, and that WDR 26 affected β‐catenin levels. In addition, WDR 26/Axin binding is involved in the ubiquitination of β‐catenin. These results suggest that WDR 26 plays a negative role in β‐catenin degradation in the Wnt signaling pathway.