Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3
Copyright policy )Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3
The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death.
- Nagoya City University Japan
eRF3, Calpain, Blotting, Western, Apoptosis, X-Linked Inhibitor of Apoptosis Protein, Inhibitor of apoptosis protein, Endoplasmic Reticulum Stress, HEK293 Cells, Cell Line, Tumor, Proteolysis, Humans, Protein Isoforms, Calcium, Translation termination, Peptide Termination Factors, Protein Binding
eRF3, Calpain, Blotting, Western, Apoptosis, X-Linked Inhibitor of Apoptosis Protein, Inhibitor of apoptosis protein, Endoplasmic Reticulum Stress, HEK293 Cells, Cell Line, Tumor, Proteolysis, Humans, Protein Isoforms, Calcium, Translation termination, Peptide Termination Factors, Protein Binding
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