ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis.
- Author(s)
- Sandow, JJ; Dorstyn, L; O'Reilly, LA; Tailler, M; Kumar, S; Strasser, A; Ekert, PG;
- Details
- Publication Year 2014-03-21,Volume 21,Issue #3,Page 4675-480
- Journal Title
- Cell Death and Differentiation
- Publication Type
- Journal Article
- Abstract
- A recent report claimed that endoplasmic reticulum (ER) stress activates the ER trans-membrane receptor IRE1α, leading to increased caspase-2 levels via degradation of microRNAs, and consequently induction of apoptosis. This observation casts caspase-2 into a central role in the apoptosis triggered by ER stress. We have used multiple cell types from caspase-2-deficient mice to test this hypothesis but failed to find significant impact of loss of caspase-2 on ER-stress-induced apoptosis. Moreover, we did not observe increased expression of caspase-2 protein in response to ER stress. Our data strongly argue against a critical role for caspase-2 in ER-stress-induced apoptosis.Cell Death and Differentiation advance online publication, 29 November 2013; doi:10.1038/cdd.2013.168
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- caspase-2; ER stress; apoptosis
- Research Division(s)
- Cell Signalling And Cell Death; Molecular Genetics Of Cancer
- Publisher's Version
- https://doi.org/10.1038/cdd.2013.168
- NHMRC Grants
- NHMRC/1020363, NHMRC/1002863, NHMRC/1016701, NHMRC/1022916, NHMRC/1021456, NHMRC/1043057, NHMRC/1009145,
- Terms of Use/Rights Notice
- © 2014 ADMC Associazione Differenziamento e Morte Cellulare
Creation Date: 2014-01-14 03:36:34
Last Modified: 2015-03-26 03:36:02