Extracellular part of cadherin is calcium binding sites. Inner cell part (domain) dock with p120 (D1-catenin), β-catenin and α-catenin (in sequence. which means α-catenin is the last). α-catenin interact with actin in the cytoplasm.
The structural and functional integrity of the cadherin-catenin complex is regulated by phosphorylation. Serine/threonine phosphorylation (S or T) of β-catenin or epithelial cadherin (E-cadherin) results in increased stabilization of the cadherin-catenin complex. However, tyrosine phosphorylation (Y) of β-catenin by the cytoplasmic kinase Fer disrupts binding of β-catenin to α-catenin, whereas phosphorylation by Src or the epidermal growth factor (EGF) receptor disrupts binding of β-catenin to cadherin.
Phosphorylation of p120 by Src or Fer (both are cytoplasmic tryosine kinase, TK) results in loss of cadherin complexes from the cell surface, perhaps as a consequence of simultaneous phosphorylation of β-catenin or because p120 is a binding site for several protein tyrosine phosphatases (PTPases) that antagonize the effects of these tyrosine kinases. In general, activation of tyrosine kinases results in a loss of cadherin-mediated cell-cell adhesion and an increase in the level of cytoplasmic β-catenin (14, 15), either by direct release of β-catenin into the cytoplasm or by activating cadherin endocytosis (17). In contrast, activation of PTPases stabilizes the cadherin-catenin complex and results in increased cadherin-mediated cell-cell adhesion (18–20).
Activation of insulin-like growth factor (IGF) type II receptor leads to transfer of β-catenin to the nucleus and TCF/LEF-mediated gene transcription. (anything related with RTK may should upregulate Wnt pathway, e.g., IGF1-RTK-PI3K-Akt. Though Akt can also phosphorelate GSK-3 to induce Wnt signal)
For instance, FGFR, EGFR in the figure below can also make the cadherin-catenin complex unstable, thus release beta-catenin into the cytoplasm and upgrade WNT signal.
Zinc finger proteins of the Slug/Snail family are repressors of E-cadherin gene transcription (37–39), and their expression is activated by signaling from the fibroblast growth factor FGF-R type I, transforming growth factor–β (TGFβ1), and ErbB1 and ErbB2. Slug/Snail expression results in loss of cell-cell adhesion and increased cell migration, as well as accumulation of signaling β-catenin that may function independently of, or synergize with, Wnt signaling (40).
https://www.science.org/doi/10.1126/science.1094291
