Traction force and mechanosensing (the ability to sense mechanical attributes of the environment) are two important factors used by a cell to modify behavior during migration. Previously it was determined that the calpain small subunit, calpain 4, regulates the production of traction force independent of its proteolytic holoenzyme. A proteolytic enzyme is formed by calpain4 binding to either of its catalytic partners, calpain 1 and 2. To further understand how calpain 4 regulates traction force, we used two-hybrid analysis to identify more components of the traction pathway. We discovered that basigin, an integral membrane protein and a documented matrix-metalloprotease (MMP) inducer binds to calpain 4 in two-hybrid and pull-down assays. Traction force was deficient when basigin was silenced in MEF cells, and defective in substrate adhesion strength. Consistent with Capn4 -/- MEF cells, the cells deficient in basigin responded to localized stimuli. Together these results implicate basigin in the pathway in which calpain 4 regulates traction force independent of the catalytic large subunits.