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Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3
Author(s) -
Hashimoto Yoshifumi,
Inagaki Hiroto,
Hoshino Shin-ichi
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.041
Subject(s) - calpain , gene isoform , regulator , protease , microbiology and biotechnology , apoptosis , programmed cell death , messenger rna , translation (biology) , caspase , chemistry , biology , gene , biochemistry , enzyme
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.