Interleukin‑1β (IL‑1b) is a pleiotropic cytokine that is important in tumor progression and invasion. Matrix metalloproteinase‑9 (MMP‑9), which is a secreted matrix‑degrading enzyme, is one of the key regulators of tumor invasion and metastasis. The current report indicated that IL‑1b promotes MMP‑9 production and cell invasion in non‑metastatic MCF‑7 breast cancer cells. IL‑1b activated focal adhesion kinase (FAK) and proto‑oncogene tyrosine‑protein kinase Src (Src). Moreover, inhibiting the Src/FAK pathway reduced the IL‑1b‑induced production of MMP‑9 and cell invasion. To investigate the functional role of FAK in MMP‑9 production cell lines expressing mutant FAK in FAK knock‑out mouse fibroblasts were generated. In wild‑type FAK‑expressing cells, MMP‑9 production was induced by IL‑1b stimulation. By contrast, IL‑1b‑induced MMP‑9 production was abrogated in FAK knock‑out, FAK Y397F, FAK Y925F, and kinase dead mutant‑expressing cells. Therefore the results of the current study indicate that FAK and Src kinases are activated by IL‑1b and play a critical role in MMP‑9 production and tumor cell invasion.