Regular ArticleIdentification of Two Novel Regulated Serines in the N Terminus of β-Catenin
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Tools for investigating O-GlcNAc in signaling and other fundamental biological pathways
2024, Journal of Biological ChemistryΒeta-catenin N-terminal domain: An enigmatic region prone to cancer causing mutations
2017, Mutation Research - Reviews in Mutation Researchβ-Catenin is O-GlcNAc glycosylated at Serine 23: Implications for β-catenin's subcellular localization and transactivator function
2014, Experimental Cell ResearchCitation Excerpt :The “Yin Yang” hypothesis suggests that the relationship between O-GlcNAcylation and O-phosphorylation is as a binary regulatory system for proteins. Van Noort et al., identified β-catenin to be phosphorylated at Ser 23 by GSK3β [26]. This finding indicated that phosphorylation and O-GlcNAcylation modifications were in direct interplay at this site, suggesting a possible cross regulation of β-catenin's function by these two modifications.
The Cdc42/Rac nucleotide exchange factor protein β<inf>1</inf>Pix (PAK-interacting exchange factor) modulates β-catenin transcriptional activity in colon cancer cells evidence for direct interactionof β<inf>1</inf>Pix with β-catenin
2013, Journal of Biological ChemistryCitation Excerpt :GSK-3β- and CK1α-induced β-catenin phosphorylation promotes β-catenin ubiquitination and proteasomal degradation (6–8). Wnt ligands activate a signal transduction mechanism that inhibits both GSK-3β- and CK1α-induced β-catenin phosphorylation, thus stabilizing and freeing β-catenin from the cytoplasmic complex and allowing it to translocate to the nucleus (8, 9). Nuclear β-catenin interacts with TCF/LEF-1 family transcription factors, thereby inducing expression of key pro-proliferative genes (6, 7).
Androgens up-regulate transcription of the notch inhibitor numb in C2C12 myoblasts via wnt/β-catenin signaling to t cell factor elements in the numb promoter
2013, Journal of Biological ChemistryCitation Excerpt :We investigated the effect of this anabolic steroid on the Wnt signaling activity. Levels of total β-catenin and nuclear active β-catenin protein were examined using antibodies against total β-catenin and active β-catenin, which lack phosphorylation on the sites of Ser-37 or Thr-41, respectively (38). C2C12 cells were cultured under differentiating conditions and treated with either vehicle or nandrolone.
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