Activated rhoA, a ras-related GTP-binding protein, stimulates the formation of stress fibers, focal adhesions, and tyrosine phosphorylation in quiescent cells. The study investigates whether rho's induction of these events is due to its stimulation of contractility. It is demonstrated that lysophosphatidic acid, which activates rho, induces myosin light chain phosphorylation, precedes the formation of stress fibers and focal adhesions, and is accompanied by increased contractility. Inhibiting contractility through different mechanisms blocks rho-induced stress fibers, focal adhesions, and tyrosine phosphorylation. Additionally, inhibiting contractility causes integrins to disperse from focal adhesions as stress fibers and focal adhesions disassemble. Conversely, stimulating contractility aggregates diffusely distributed integrins into focal adhesions. These findings suggest that activated rho stimulates contractility, which drives the formation of stress fibers and focal adhesions and elevates tyrosine phosphorylation. A model is proposed to explain how contractility promotes these events.Activated rhoA, a ras-related GTP-binding protein, stimulates the formation of stress fibers, focal adhesions, and tyrosine phosphorylation in quiescent cells. The study investigates whether rho's induction of these events is due to its stimulation of contractility. It is demonstrated that lysophosphatidic acid, which activates rho, induces myosin light chain phosphorylation, precedes the formation of stress fibers and focal adhesions, and is accompanied by increased contractility. Inhibiting contractility through different mechanisms blocks rho-induced stress fibers, focal adhesions, and tyrosine phosphorylation. Additionally, inhibiting contractility causes integrins to disperse from focal adhesions as stress fibers and focal adhesions disassemble. Conversely, stimulating contractility aggregates diffusely distributed integrins into focal adhesions. These findings suggest that activated rho stimulates contractility, which drives the formation of stress fibers and focal adhesions and elevates tyrosine phosphorylation. A model is proposed to explain how contractility promotes these events.