CBL-like E3 ubiquitin ligase Hakai (CBLL1) binds to SRC-phosphorylated E-cadherin (CDH1) complex bound to Listeria monocytogenes cell wall protein InlA (Bonazzi et al. 2008). SRC-mediated phosphorylation of CDH1 complex on tyrosine residues Y753 and Y754 of CDH1 and an unknown tyrosine of beta-catenin (CTNNB1) at cell-cell adhesion sites creates docking sites for CBLL1. CBLL1 functions as zinc (Zn2+) coordinated homodimer. While CBLL1 interacts simultaneously with CDH1 and CTNNB1, CTNND1 (p120 catenin) is displaced by CBLL1 binding (Fujita et al. 2002, Mukherjee et al. 2012).