Schematic model of tensin3 recruitment to CMAs and the maturation of focal adhesions to fibrillar adhesions. At the cell periphery actomyosin links integrins to adhesion complexes through talin and vinculin to form FAs. Tensin joins this complex in FAs where it binds to talin and other adhesion complex proteins including integrins. Forces through actin binding to the mechanosensors talin/vinculin will cause the translocation of tensin to more central locations in the cell. This translocation depends on (i) tensin binding to talin via the talin binding site located in the tensin IDR, which engages R11 in the talin rod and (ii) the substrate rigidity, whereby fibronectin that associates with α5β1 integrins favours fibrilogenesis when cells encounter more pliable substrates. We speculate that binding of tensin3 to the cytoplasmic domain of α5β1 integrins competes with talin binding to integrins which then leads to a reduction of forces acting on the adhesion proteins, as observed in experiments using vinculin (LaCroix et al., 2018) or talin (Kumar et al., 2016) tension sensor constructs. The gradual reduction of forces across either of these mechanosensitive proteins may lead to their disassociation from centrally located adhesions, thus reducing the integrin-actin axis via the mechanosensors. In contrast, tensin3 remains present at FBs maintaining α5β1 integrins in an active, ligand-engaged state (Georgiadou et al., 2017) independently of tension. As such, there is a hand-over of talin-integrin to tensin3-integrin, resulting from the reduction of forces across the mechanosensitive talin molecule. The resulting stable integrin-tensin enriched structures remain attached to fibronectin fibrils and may represent a signalling hub that remains active to uphold tension-independent integrin-mediated cell-matrix communication processes required to maintain tissue function.