Model of a migrating cell containing diverse integrin-based adhesion structures that transmit different levels of traction forces. Nascent adhesions (NAs) emerge at the leading edge of cell protrusions by nucleating multiple ligand-bond integrins that have been activated by talin and kindlin. Adhesome proteins such as vinculin are subsequently recruited to adhesion sites via talin in a tension-dependent manner or via paxillin in a tension-independent manner. NAs are dynamically coupled to the polymerizing branched actin network through proteins of the molecular clutch such as talin and vinculin, which convert the retrograde movement of polymerizing branched actin network into a protrusive force at the leading edge membrane and rearward traction force on the ECM. A small number of NAs matures into large focal adhesions (FAs) along actomyosin bundles in the lamella. Within mature FAs, the molecular clutch becomes strongly engaged by F-actin binding to the talin ABS2 and ABS3 sites and vinculin binding to VBS where high traction forces are transmitted across integrins, leading to catch bond formation between integrin and ligand. Behind the lamella, Kank2 is recruited to the FA belt, where it maintains talin in its active integrin-bond state and at the same time diminishes F-actin binding to talin ABS2. Consequently, Kank2 decreases force transmission leading to the slip bond formation between integrin and its ligand and the translocation of FA belt-localized β1 integrins into fibrillar (or central) adhesions. At the rear end of migrating cells, trailing edge FAs may apply such high traction forces that detach the cell rear, probably together with integrin-bound ECM fragments.