TP53 regulated inhibitor of apoptosis 1 (TRIAP1)

TP53 regulated inhibitor of apoptosis 1 (TRIAP1) is a mitochondrial protein encoded by the TRIAP1 gene, induced in response to cellular stress and p53 activation. It localizes to the mitochondrial intermembrane space, where it acts as a chaperone-like scaffold that binds PRELI-like domain proteins, crucial for the transfer of phosphatidic acid required for cardiolipin biosynthesis. Functionally, TRIAP1 modulates mitochondrial apoptosis by inhibiting activation of caspase-9, thus promoting cell survival after p53-mediated stress signals. Structurally, it features a twin CX9C motif that forms a disulfide-stabilized helical bundle; its distinct hydrophobic surface mediates key protein-protein interactions. TRIAP1 has been implicated in the development and progression of certain cancers and kidney diseases but is not currently a direct therapeutic target with known selective drugs.

Other names

TP53-regulated inhibitor of apoptosis 1TRIAP115E1.1HSPC132p53CSVP53CSVWF-1MDM35Protein 15E1.1p53-inducible cell-survival factormitochondrial distribution and morphology 35 homolog (S. cerevisiae)

Inhibition of apoptosis by preventing caspase-9 activation. Supports mitochondrial integrity by facilitating cardiolipin synthesis through phosphatidic acid transport as part of the TRIAP1:PRELID complex.