The deregulation of cell growth and cell migration leads to cancer. Migration from the primary tumour into the surrounding tissue is a critical step in the course of the disease. Directed cell migration depends on cellular asymmetry and the arrangement of forces generated in different regions of the cell. Fine-tuned cytosolic Ca²⁺ signals that are critical for coordinating these forces originate among others from Ca²⁺ channels involved in mechanosensation. In this regard, the classical transient receptor potential-1 (TRPC1) channel is debated as a possible candidate. We analyzed its function in transformed renal epithelial (MDCK-F) cells which underwent epithelial-mesenchymal transformation like carcinoma cells. We show here that activity of TRPC1 is crucial for fibroblast growth factor 2 (FGF2) induced cell migration. Silencing of TRPC1 activity by means of RNA interference or pharmacologically with GsMTx-4 impairs chemotaxis. Reducing TRPC1 channel activity blocks directed cell migration as efficiently as does inhibition of particular steps of growth factor-induced signaling like phospholipase C or phosphatidyl-inositol-3-OH kinase. Whole-cell patch-clamp recordings show an increase in TRPC1-mediated currents in response to FGF2 stimulation. The functional connection is correlated with clustering of FGF-receptors with TRPC1 channels in signaling platforms as observed by immunolabeling. This suggests that TRPC1 might equip a migrating cell with information of its position within an FGF2 gradient.