Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis
Copyright policy )Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis
Significance The release of cytochrome c from its normal intermembrane space in mitochondria marks the initiation of apoptosis in mammalian cells. The process is triggered by the aggregation of B-cell leukemia/lymphoma 2 (BCL2)-associated X (Bax) and BCL2-antagonist/killer (Bak) proteins on the surface of mitochondria. We found that a mitochondrial inner membrane protease, OMA1 (overlapping activity with m -AAA protease), is specifically activated and is responsible for cleaving another inner membrane protein, optical nerve atrophy 1 (OPA1), upon Bax/Bak aggregation. The cleavage of OPA1 triggers the remodeling of mitochondrial cristae, allowing the majority of cytochrome c inside the cristae to be released. This finding provided a more comprehensive understanding of this critical molecular event during apoptosis.
- Chinese Academy of Medical Sciences & Peking Union Medical College China (People's Republic of)
- PEKING UNION MEDICAL COLLEGE China (People's Republic of)
- National Institute of Biological Sciences, Beijing China (People's Republic of)
Protein Stability, Cytochromes c, Metalloendopeptidases, Apoptosis, GTP Phosphohydrolases, Mitochondria, Enzyme Activation, bcl-2 Homologous Antagonist-Killer Protein, Cell Line, Tumor, Gene Knockdown Techniques, Humans, BH3 Interacting Domain Death Agonist Protein, bcl-2-Associated X Protein
Protein Stability, Cytochromes c, Metalloendopeptidases, Apoptosis, GTP Phosphohydrolases, Mitochondria, Enzyme Activation, bcl-2 Homologous Antagonist-Killer Protein, Cell Line, Tumor, Gene Knockdown Techniques, Humans, BH3 Interacting Domain Death Agonist Protein, bcl-2-Associated X Protein
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