Accumulation of integrin receptor proteins and their binding to ECM ligand molecules promote activation of FAK,[34] where FAK dimerization induces auto‐phosphorylation at Tyr397 with Src.[12] Overexpressed FAK, acting as a major integrin‐mediated intracellular signaling kinase in ovarian[35] and breast cancers,[36] is attributed to FAK‐dependent invasion and metastatic potential.[37] As previous results confirmed that regulation of cell spreading by micropatterning altered intracellular cytoskeletal tension,[38] cell‐ECM binding force modulated cell spreading (Figure 1). This evidence concerns the gene PTK2 and breast cancer.