Inhibitor of Apoptosis Proteins Are Substrates for the Mitochondrial Serine Protease Omi/HtrA2
Copyright policy )Inhibitor of Apoptosis Proteins Are Substrates for the Mitochondrial Serine Protease Omi/HtrA2
The mature serine protease Omi/HtrA2 is released from the mitochondria into the cytosol during apoptosis. Suppression of Omi/HtrA2 by RNA interference in human cell lines reduces cell death in response to TRAIL and etoposide. In contrast, ectopic expression of mature wildtype Omi/HtrA2, but not an active site mutant, induces potent caspase activation and apoptosis. In vitro assays demonstrated that Omi/HtrA2 could degrade inhibitor of apoptosis proteins (IAPs). Consistent with this observation, increased expression of Omi/HtrA2 in cells increases degradation of XIAP, while suppression of Omi/HtrA2 by RNA interference has an opposite effect. Combined, our data demonstrate that IAPs are substrates for Omi/HtrA2, and their degradation could be a mechanism by which the mitochondrially released Omi/HtrA2 activates caspases during apoptosis.
- Thomas Jefferson University United States
Base Sequence, Serine Endopeptidases, Proteins, Apoptosis, X-Linked Inhibitor of Apoptosis Protein, High-Temperature Requirement A Serine Peptidase 2, Cell Line, Mitochondria, Substrate Specificity, Enzyme Activation, Mitochondrial Proteins, Caspases, Humans, RNA Interference, DNA Primers
Base Sequence, Serine Endopeptidases, Proteins, Apoptosis, X-Linked Inhibitor of Apoptosis Protein, High-Temperature Requirement A Serine Peptidase 2, Cell Line, Mitochondria, Substrate Specificity, Enzyme Activation, Mitochondrial Proteins, Caspases, Humans, RNA Interference, DNA Primers
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