Gene interactions and pathways from curated databases and text-mining

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CTNNB1 — SOX9

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Akiyama et al., Genes Dev 2004 : Sox9 markedly inhibits activation of beta-catenin dependent promoters and stimulates degradation of beta-catenin by the ubiquitination/proteasome pathway
Blache et al., J Cell Biol 2004 (Carcinoma...) : We provide in vitro and in vivo evidence that a bipartite beta-catenin/TCF4 transcription factor, the effector of the Wnt signaling pathway, is required for SOX9 expression in epithelial cells
Wang et al., Cancer Res 2007 (Neoplasm Recurrence, Local...) : SOX9 message and protein levels in prostate cancer cells were increased by treatment with glycogen synthase kinase 3beta inhibitor ( SB415286 ), and SOX9 was reduced when beta-catenin was down-regulated by small interfering RNA ( siRNA ), indicating that SOX9 expression in prostate cancer is regulated by Wnt/beta-catenin signaling
Bastide et al., J Cell Biol 2007 : Sox9 expression requires an active beta-catenin-Tcf complex, the transcriptional effector of the Wnt pathway
Wang et al., Cancer Res 2008 (Neoplasm Invasiveness...) : Moreover, SOX9 expression in PCa cell lines enhanced tumor cell proliferation and was beta-catenin regulated
Topol et al., J Biol Chem 2009 : Chondrocyte fate determination and maintenance requires Sox9 , an intrinsic transcription factor, but is inhibited by Wnt/beta-catenin signaling activated by extrinsic Wnt ligands ... We found that Sox9 employed two distinct mechanisms to inhibit Wnt/beta-catenin signaling : the Sox9 N terminus is necessary and sufficient to promote beta-catenin degradation, whereas the C terminus is required to inhibit beta-catenin transcriptional activity without affecting its stability ... Independent of its DNA binding ability, nuclear localization of Sox9 is both necessary and sufficient to enhance beta-catenin phosphorylation and its subsequent degradation