Desmoglein-2

Desmoglein2 is one of three members of the desmoglein subfamily of calcium-dependent cadherin cell adhesion molecules. Together with desmocollins, another subfamily within the cadherin superfamily, the desmoglein isoforms form the adhesive components of desmosomes, the cell-cell adhesive structures that are found in epithelial cells. Human Desmoglein2 is a type I transmembrane glycoprotein of 1117 amino acid (aa) residues with a 23 aa signal peptide and a 25 aa propeptide. It differs from other classic cadherins by having four instead of five cadherin repeat domains in its extracellular region, and a much larger cytoplasmic region containing five desmoglein repeat domains which share homology with the cadherin repeats. Instead of having the HAV adhesion motif found in type I cadherins, desmogleins have R/YAL as the adhesion motif on its aminoterminal cadherin repeat. The cytoplasmic tails of desmogleins interact with desmoplakins, plakoglobin and plakophilins. In turn, these proteins link the desmogleins with the intermediate filaments. Desmoglein2 has been shown to be important in establishing cellcell adhesion and function in epithelial cells. Desmoglein2 was originally identified in colon carcinoma and colon, and was named HDGC (human desmoglein colon) .