Background information
Cadherins comprise a family of Ca++-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins each contain a large extracellular domain at the amino-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short carboxy-terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including beta-catenin, to regulate cadherin function. Cadherin-26 is a 852 amino acid single-pass transmembrane protein containing 4 cadherin domains through which it interacts with other cadherins in a homophilic manner. There are 4 named isoforms of cadherin-26 that are produced as a result of alternative spicing events.
