The formation of tissues and organs of multicellular organisms during embryonic development involves a highly regulated process of integration and segregation of heterogeneous cell populations into organised cell patterns.¹ One of the major regulators of the processes of cell migration, proliferation, and differentiation during organogenesis is cell-cell adhesion, which is predominantly mediated by cell surface glycoproteins. These cell adhesion proteins can respond to cell signalling events and can also transduce signals into the cell.² Four major groups of cell adhesion proteins have been described, including integrins, immunoglobulins, selectins, and cadherins.

Cadherins are a superfamily of integral membrane proteins that are subdivided into six gene families.¹ E-cadherin, a member of the classical cadherin type I family, has been widely studied in a variety of epithelial cell systems.^2–5 Like most cadherins, E-cadherin is a transmembrane glycoprotein with an extracellular domain that interacts with the extracellular domains of cadherin molecules of adjacent cells in a calcium dependent homophilic manner. The highly conserved intracellular (cytoplasmic) domain of E-cadherin functions as a binding site for catenins (cytoplasmic proteins that anchor E-cadherin to the cell cytoskeleton). Typically, E-cadherin binds to β-catenin or p120 catenin in the cells; these catenins in turn are associated with α-catenin which links the cadherin-catenin complex to the cytoskeletal protein F-actin within the cell. The formation of cadherin-catenin complexes is critical to cell-cell adhesion. Both cadherins and …