ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis
Cell Death & Differentiation, 2014•nature.com
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 …
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 …
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.
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