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Cell Death Differ. 2014 Mar;21(3):475-80. doi: 10.1038/cdd.2013.168. Epub 2013 Nov 29.

ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis.

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1] The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia [2] Department of Medical Biology, The University of Melbourne, Parkville, VIC 3052, Australia.
1] The Centre for Cancer Biology, SA Pathology, Adelaide, SA 5000, Australia [2] Department of Medicine, University of Adelaide, Adelaide, SA 5005, Australia [3] Division of Health Sciences, University of South Australia, Adelaide, SA 5001, Australia.


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.

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