Adhesion proteins function in confined spaces between cells or between cells and extracellular matrix. Using cadherins as model adhesion proteins, studies tested the postulate that confinement within quasi two-dimensional intercellular gaps enhances protein-protein interactions that are not detected in solution (3D). Micropipette-based measurements of cadherin-mediated cell-cell binding kinetics identified a unique kinetic signature that reflects both adhesive (trans) bonds between cadherins on opposing cells and putative lateral (cis) interactions between cadherins on the same cell. In solution, the adhesive extracellular domains only form trans bonds in solution (3D). Mutations postulated to disrupt the lateral interactions altered the kinetic signatures, but did not affect the trans binding affinity. The kinetic signatures further correlated with cadherin organization at cell-cell junctions, with altered wound healing dynamics, and with the macromolecular permeability of inter epithelial junctions. These measurements thus revealed confinement-enhanced, quantifiable cadherin interactions that both influence adhesion protein organization within intercellular gaps and regulate tissue functions.

Recognition in tight spaces

251st National Meeting (2016)

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