Ontology highlight
ABSTRACT:
SUBMITTER: Goto T
PROVIDER: S-EPMC5084729 | biostudies-literature | 2016 May
REPOSITORIES: biostudies-literature
Goto Toshiyasu T Matsuzawa Junhei J Iemura Shun-Ichiro S Natsume Tohru T Shibuya Hiroshi H
FEBS letters 20160503 9
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 WDR ...[more]