Cadherins comprise a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. The classical cadherins, E-, N- and P-cadherin, consist of large extracellular domains characterized by a series of five homologous NH2 terminal repeats. The most distal of these cadherins is thought to be responsible for binding specificity, transmembrane domains and carboxy-terminal intracellular domains. The relatively short intracellular domains interact with a variety of cytoplasmic proteins, such as b-catenin, to regulate cadherin function. Members of this family of adhesion proteins include rat cadherin K (and its human homolog, cadherin-6), R-cadherin, B-cadherin, E/P cadherin and cadherin-5.
