Lateral Mobility of E-Cadherin Enhances Rac1 Response in Epithelial Cells

The fluidity of cellular membranes imparts lateral mobility of proteins across the cell surface. To understand the impact of lateral mobility on cell-cell communication, a protein consisting of the extracellular recognition domains of E-cadherin was associated with the surface of silica beads by either tethering to a bead-supported lipid bilayer or direct adsorption, resulting in laterally mobile and immobile presentations of this protein. These beads were then seeded onto the upper surface of MDCK cells. Functional engagement of these beads was compared by measurement of Rac1 recruitment around the bead. Lateral mobility enhanced recognition of E-cadherin, promoting cell response to the beads at lower per-area concentrations than their immobilized counterparts. A more complete understanding of how lateral mobility of membrane-associated proteins influences molecular recognition, and potentially other downstream responses, could provide new strategies for the design of materials and devices intended to capture the architecture of natural tissues.