Journal article
ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis
JJ Sandow, L Dorstyn, LA O'Reilly, M Tailler, S Kumar, A Strasser, PG Ekert
Cell Death and Differentiation | Published : 2014
DOI: 10.1038/cdd.2013.168
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. © 2014 Macmillan ..
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Awarded by Leukemia and Lymphoma Society
Funding Acknowledgements
We are grateful to Drs D Vaux, J Adams, J Silke, G Dewson and F Ke for helpful comments, cells and reagents. This work was supported by NHMRC Senior Principal Research Fellowships to AS (1020363), and SK (1002863), a South Australian Cancer Research Collaborative Fellowship (LD), and by program grant (1016701) and project grants (1022916, 1021456, 1043057 and 1009145) from the NHMRC (Australia), a SCOR grant (7417-07) from the Leukemia and Lymphoma Society, Victorian State Government Operational Infrastructure Support and the Australian Government NHMRC Independent Research Institute Infrastructure Support Scheme.