PDCD8/AIFM1 Protein, Human (His)

PDCD8/AIFM1 protein exhibits dual functionality, serving as both an NADH oxidoreductase and a regulator of apoptosis. In response to apoptotic stimuli, it undergoes translocation from the mitochondrial intermembrane space to the cytosol and nucleus, functioning as a proapoptotic factor through a caspase-independent pathway. This release into the cytoplasm is facilitated by its binding to poly-ADP-ribose chains. The soluble form (AIFsol) found in the nucleus induces 'parthanatos,' characterized by caspase-independent fragmentation of chromosomal DNA. Additionally, PDCD8/AIFM1 interacts with EIF3G, inhibiting the EIF3 machinery and protein synthesis while activating caspase-7 to amplify apoptosis. It plays a critical role in caspase-independent, pyknotic cell death induced by hydrogen peroxide. In normal mitochondrial metabolism, PDCD8/AIFM1 contributes significantly to the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import. Notably, PDCD8/AIFM1 demonstrates NADH oxidoreductase activity and does not induce nuclear apoptosis.