A structural view of cadherin adhesion

Summary form only. The cadherins comprise the largest known family of cell adhesion proteins, and their function is critical in countless events in the morphogenesis and homeostasis of solid tissues. Nonetheless, the molecular mechanisms underlying cadherin-mediated cell adhesion and its regulation are only partly understood. We present data from cell adhesion studies which suggest that adhesion in classical cadherins is mediated primarily through the amino-terminal domain. This data supports similar conclusions from numerous previous studies. Furthermore, we present crystallographic evidence that explains some aspects of cell adhesion at the atomic level, in particular that cis- (same cell) dimerization is a prerequisite for activation of cadherin adhesion, and may operate by increasing the homophilic avidity of cadherins by a mechanism akin to clustering.