Calpain mediates processing of the translation termination factor eRF3 into the IAP-binding isoform p-eRF3.
Yoshifumi Hashimoto, Hiroto Inagaki, Shin-ichi Hoshino
Index: FEBS Lett. 589 , 2241-7, (2015)
Full Text: HTML
Abstract
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. Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Related Compounds
Related Articles:
Detailed characterization of a long-term rodent model of critical illness and recovery.
2015-03-01
[Crit. Care Med. 43(3) , e84-96, (2015)]
2015-01-01
[PLoS ONE 10(3) , e0119423, (2015)]
2015-01-01
[Clin. Exp. Hypertens. 37(2) , 136-41, (2015)]
Hydrogel-assisted functional reconstitution of human P-glycoprotein (ABCB1) in giant liposomes.
2015-02-01
[Biochim. Biophys. Acta 1848(2) , 643-53, (2014)]
2015-04-01
[Inflammation 38(2) , 672-82, (2015)]