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J Biol Chem 2000 Oct 20;27542:32871-8. doi: 10.1074/jbc.M004089200.
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A novel beta-catenin-binding protein inhibits beta-catenin-dependent Tcf activation and axis formation.

Sakamoto I , Kishida S , Fukui A , Kishida M , Yamamoto H , Hino S , Michiue T , Takada S , Asashima M , Kikuchi A .

beta-Catenin is efficiently phosphorylated by glycogen synthase kinase-3beta in the Axin complex in the cytoplasm, resulting in the down-regulation. In response to Wnt, beta-catenin is stabilized and translocated into the nucleus where it stimulates gene expression through Tcf/Lef. Here we report a novel protein, designated Duplin (for axis duplication inhibitor), which negatively regulates the function of beta-catenin in the nucleus. Duplin was located in the nucleus. Duplin bound directly to the Armadillo repeats of beta-catenin, thereby inhibiting the binding of Tcf to beta-catenin. It did not affect the stability of beta-catenin but inhibited Wnt- or beta-catenin-dependent Tcf activation. Furthermore, expression of Duplin in Xenopus embryos inhibited the axis formation and beta-catenin-dependent axis duplication, and prevented the beta-catenin''s ability to rescue ventralizing phenotypes induced by ultraviolet light irradiation. Thus, Duplin is a nuclear protein that inhibits beta-catenin signaling.

PubMed ID: 10921920
Article link: J Biol Chem

Species referenced: Xenopus laevis
Genes referenced: chd8 ctnnb1 gys1 sia1 supt16h trak2 wnt8a

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