R-Cadherin

The classic cadherins are homophilic adhesion molecules. That is, E-cadherin expressed on one cell surface binds to E-cadherin expressed on an apposed cell surface, N-cadherin binds to N, P to P and so forth. It was originally thought that all cadherins would behave completely homophilically but it is now clear that, for example, N-cadherin can bind to R-cadherin, although perhaps more weakly than it would to N-cadherin. 

Recently, several novel members of the cadherin family have been discovered M-cadherin in mouse embryonic skeletal muscle [35,36], R-cadherin in neuronal cells [37] and T-cadherin in myoblasts [38]. The structure of T-cadherin (Fig. 4) is of special interest. This cadherin in its mature form lacks the transmembrane and cytoplasmic domains of classical cadherins and is integrated into the membrane by a GPl anchor. Although T-cadherin is a severely truncated form and additionally lacks an HAV sequence in the El domain it appears to be functional. Transfection of cDNA encoding T-cadherin into a cell devoid of cadherin expression confers calcium-dependent aggregation on the cells [38]. The mechanism of T-cadherin adhesion is intriguing and presumably is independent of interactions with catenins and direct coupling with actin filaments. 

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