Ezh2 interaction with VEC was confirmed in vivo in mouse lung extracts in the absence of any crosslinking reaction, whereas no association was detected between Ezh2 and the other major classical endothelial cadherin, N-cadherin, likely as a result of the reduced binding of this adhesion molecule to p120-catenin.42 Recently, EZH2 has been shown to interact with β-catenin in liver cancer stem cells43 through its N-terminal domain (amino acids 1–334). This evidence concerns the gene CTNND1 and liver cancer.