Schematic model of tensin3 LLPS in response to rigidity sensing. Schematic model of tensin3 recruitment to adhesions and its response to the surrounding mechanical environment. At the cell periphery, talin and other integrin activators (e.g., kindlin) activate integrins at the cell–ECM contact to form adhesion complexes. While talin and vinculin bind to actin filaments, actomyosin-mediated force induces the maturation of FAs with enrichment of α5β1 and αvβ3 integrins. The development of FAs into FBs depends on both substrate stiffness and the binding of tensin3 to talin. On stiff substrates, actomyosin-mediated forces stabilize talin in an active conformation that retains multiple tensin3 molecules during FA maturation into FBs. Tensin3 regulates integrin activity through its interactions with talin and integrins, which control the formation of force-independent stable FBs. On soft substrates, talin experiences lower forces and therefore exposes fewer binding sites for tensin3. Such reduced tensin3 retention in adhesions results in the formation of fewer FBs (Barber-Pérez et al., 2020) and increased tensin3 phase separation into biomolecular condensates. The tensin3 condensates could serve as storage compartments for adhesion proteins (e.g., talin) and initiate signaling (e.g., DLC1 and GIGYF1).