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Fig. 3 | Cancer Cell International

Fig. 3

From: Triple-negative breast cancer: understanding Wnt signaling in drug resistance

Fig. 3

Schematic overview of β-catenin–MUC1 dynamics. MUC1 interacts with various receptor tyrosine kinases, such as EGFR, FGFR, PDGFR, and HER2. When the serine-rich domain of MUC1-C is phosphorylated by EGFR or cSRC, the affinity for β-catenin binding is increased. Following cleavage of the cytoplasmic domain, the MUC1/β- catenin complex localizes adjacent to the membrane and binds cytoskeleton members (fascin and vinculin), or competitively binds with E-cadherin to prevent E-cadherin/β-catenin complex formation. The formation of the MUC1/β-catenin complex stabilizes β-catenin in the cytoplasm by preventing its phosphorylation-mediated proteasomal degradation. In addition, MUC1-CD/β-catenin is translocated into the nucleus and interacts with (TCF7L2/TCF4) transcription factors to activate Wnt-triggered genes transcription

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