The atomic structure of myosin-S1 suggests that its working stroke, which generates tension and shortening in muscle, is triggered by the release of inorganic phosphate from the active site. This mechanism is the basis of a new mechanokinetic model for contractility, using the biochemical actomyosin ATPase cycle, strain-dependent kinetics and dimeric myosins on buckling rods. In this model, phosphate-dependent aspects of contractility arise from a rapid reversible release of phosphate from the initial bound state (A.M.ADP.Pi), which triggers the stroke. Added phosphate drives bound myosin towards this initial state, and the transient tension response to a phosphate jump reflects the rate at which it detaches from actin. Predictions for the tensile and energetic properties of striated muscle as a function of phosphate level, including the tension responses to length steps and Pi-jumps, are compared with experimental data from rabbit psoas fibres at 10 °C. The phosphate sensitivity of isometric tension is maximal when the actin affinity of M.ADP.Pi is near unity. Hence variations in actin affinity modulate the phosphate dependence of isometric tension, and may explain why phosphate sensitivity is temperature-dependent or absent in different muscles.