Through actomyosin stress fibres (SFs), cells apply tensile forces on their surroundings – in particular at focal adhesions (FAs). Some FA proteins can act as mechanosensors and undergo conformational changes upon the application of force, but it remains unclear how tensile force in an individual SF is distributed and contributes to tensile homeostasis between the cytoskeleton and the extracellular matrix. On page 3021, Ching-Wei Chang and Sanjay Kumar address these questions by severing single SFs in cells with femtosecond lasers and tracking the tension across the FA protein vinculin with a vinculin tension sensor. They find that severing a single SF leads to an overall decrease in vinculin tension but, surprisingly, tension is not reduced in a uniform manner; vinculin tension is decreased in FAs that are aligned with the severed SFs but can also be increased in many others that are not. In addition, central and peripheral SFs produce different distributions of vinculin tension; severing of peripheral SFs results in a greater overall tension reduction transmitted to FAs in comparatively limited regions, whereas ablation of central SFs transmits tension in a highly dynamic and delocalized fashion. These results suggest that central SFs are structurally interconnected, which helps to dissipate the tension to vinculin mechanosensors when they are severed; however, disruption of peripheral SFs produces a narrower spatial redistribution of tension, accompanied by FA rupture and cell shape change.