Unknown

Dataset Information

0

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


ABSTRACT: The stability of ?-catenin is very important for canonical Wnt signaling. A protein complex including Axin/APC/GSK3? phosphorylates ?-catenin to be degraded by ubiquitination with ?-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 ?-catenin levels. In addition, WDR26/Axin binding is involved in the ubiquitination of ?-catenin. These results suggest that WDR26 plays a negative role in ?-catenin degradation in the Wnt signaling pathway.

SUBMITTER: Goto T 

PROVIDER: S-EPMC5084729 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

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]

Similar Datasets

| S-EPMC9190513 | biostudies-literature
| S-EPMC3967064 | biostudies-literature
| S-EPMC4922628 | biostudies-literature
| S-EPMC4094682 | biostudies-literature
| S-EPMC4106995 | biostudies-literature
| S-EPMC8176142 | biostudies-literature
| S-EPMC6021530 | biostudies-literature
| S-EPMC3988066 | biostudies-literature
| S-EPMC3676431 | biostudies-literature
| S-EPMC7785591 | biostudies-literature