An unusual mechanism controls the adhesive failure of bonds between cadherin extracellular domains

The authors examined the forces that control the adhesive behavior of cadherin ectodomains from Xenopus. Using the surface force apparatus, they measured directly the force between oriented, cadherin monolayers as a function of their separation distance. They established previously that cadherin can bind in multiple antiparallel configurations, which involve different regions of the protein. They show that, on account of these interactions, the failure of homophilic cadherin junctions is marked by an unusual unbinding profile that appears to be caused by the hopping between successive minima along the unbinding trajectory. These findings suggest that these multiple adhesive contacts may have evolved in order to impede the abrupt failure of cadherin-mediated cell-cell adhesion