In the cancer cell mitochondria, but not in normal cell mitochondria, HSP60 also directly binds with cyclophilin D (CypD), a mitochondrial permeability transition pore component in a multi-chaperone complex also containing HSP90 and Tumor Necrosis Factor Receptor-Associated Protein-1 (TRAP-1), Genetic silencing of HSP60 has shown to induce CypD-dependent mitochondrial permeability transition, caspase-dependent apoptosis and tumor growth suppression, suggesting HSP60 as a novel regulator of a cytoprotective chaperone network inhibiting CypD-dependent tumor cell death [164]. This evidence concerns the gene HSP90AA1 and cancer.