TRIAP1 (TP53 regulated inhibitor of apoptosis 1) is a mitochondrial protein with dual functions in lipid trafficking and apoptosis suppression. Mechanistically, TRIAP1 forms complexes with PRELID1 and PRELID3A to facilitate phosphatidic acid (PA) transfer across the mitochondrial intermembrane space, enabling cardiolipin synthesis essential for mitochondrial membrane integrity 12. TRIAP1 inhibits intrinsic apoptosis by preventing caspase-9 activation and retaining cytochrome c within mitochondria 34. Its folding is uniquely constrained by functional requirements, involving a redox-controlled pathway where MIA40 catalyzes proper disulfide bond formation to maintain the protein's dual cytosolic and mitochondrial roles 5. Clinically, TRIAP1 dysregulation drives multiple cancers. In colorectal cancer, YY1 transcriptionally activates TRIAP1 to promote proliferation and metastasis 6, while TRIAP1 depletion impairs cancer cell adaptation to glutamine deprivation via p53-mediated stress 7. In osteosarcoma, epirubicin chemosensitivity requires miR-1301-mediated TRIAP1 downregulation 8. TRIAP1 overexpression confers resistance to microtubule-targeting drugs by reducing DNA damage 4. In non-small cell lung cancer, TRIAP1 maintains radioresistance through redox homeostasis regulation 9. TRIAP1 is identified as a prognostic marker in multiple myeloma 10, and exercise-induced mitochondrial immune signaling involves TRIAP1 downregulation 11.