Glycocalyx around integrin–ligand complexes promotes integrin–ligand binding and clustering. The glycocalyx is a layer of glycoprotein–polysaccharide complexes on the cell surface that exerts electrosteric and osmotic repulsion to the ECM. Because the height of the glycocalyx exceeds that of the active integrins, the glycocalyx must be mechanically compressed around integrin–ligand complexes (indicated as blue arrows). Ligand-bound integrins within the compressed glycocalyx reciprocally sense the pulling force that promotes catch-bond formation and mechanotransduction. Glycocalyx-embedded integrin–ligand complexes shorten the distance between the plasma membrane and the ECM, which increases the probability of integrin activation and clustering around existing integrin-based adhesion sites in a kinetic trap-like manner. Talin is immobilized by actomyosin bundles within FAs, where it captures and activates integrins that enter the kinetic trap.