ZFIN ID: ZDB-PUB-040920-3
Essential role of BCL9-2 in the switch between β-catenin's adhesive and transcriptional functions
Brembeck, F.H., Schwarz-Romond, T., Bakkers, J., Wilhelm, S., Hammerschmidt, M., and Birchmeier, W.
Date: 2004
Source: Genes and Development 18(18): 2225-2230 (Journal)
Registered Authors: Bakkers, Jeroen, Hammerschmidt, Matthias
Keywords: BCL9/legless; beta-catenin; Wnt8; tyrosine phosphorylation; epithelial–mesenchymal transition; mesoderm patterning
MeSH Terms: Animals; Body Patterning; Carrier Proteins/physiology*; Cell Adhesion/physiology; Cell Line, Transformed (all 31) expand
PubMed: 15371335 Full text @ Genes Dev.
beta-Catenin controls both cadherin-mediated cell adhesion and activation of Wnt target genes. We demonstrate here that the beta-catenin-binding protein BCL9-2, a homolog of the human proto-oncogene product BCL9, induces epithelial-mesenchymal transitions of nontransformed cells and increases beta-catenin-dependent transcription. RNA interference of BCL9-2 in carcinoma cells induces an epithelial phenotype and translocates beta-catenin from the nucleus to the cell membrane. The switch between beta-catenin's adhesive and transcriptional functions is modulated by phosphorylation of Tyr 142 of beta-catenin, which favors BCL9-2 binding and precludes interaction with alpha-catenin. During zebrafish embryogenesis, BCL9-2 acts in the Wnt8-signaling pathway and regulates mesoderm patterning.