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.
Mesh Terms:
Blotting, Western, Calcium, Calpain, Cell Line, Tumor, Endoplasmic Reticulum Stress, HEK293 Cells, Humans, Peptide Termination Factors, Protein Binding, Protein Isoforms, Proteolysis, X-Linked Inhibitor of Apoptosis Protein
Blotting, Western, Calcium, Calpain, Cell Line, Tumor, Endoplasmic Reticulum Stress, HEK293 Cells, Humans, Peptide Termination Factors, Protein Binding, Protein Isoforms, Proteolysis, X-Linked Inhibitor of Apoptosis Protein
FEBS Lett.
Date: Aug. 04, 2015
PubMed ID: 26172506
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