Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/106152
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Type: Journal article
Title: DR5 and caspase-8 are dispensable in ER stress-induced apoptosis
Author: Glab, J.
Doerflinger, M.
Nedeva, C.
Jose, I.
Mbogo, G.
Paton, J.
Paton, A.
Kueh, A.
Herold, M.
Huang, D.
Segal, D.
Brumatti, G.
Puthalakath, H.
Citation: Cell Death and Differentiation, 2017; 24(5):944-950
Publisher: Nature Publishing Group
Issue Date: 2017
ISSN: 1350-9047
1476-5403
Statement of
Responsibility: 
Jason A Glab, Marcel Doerflinger, Christina Nedeva, Irvin Jose, George W Mbogo, James C Paton, Adrienne W Paton, Andrew J Kueh, Marco J Herold, David CS Huang, David Segal, Gabriella Brumatti, and Hamsa Puthalakath
Abstract: The endoplasmic reticulum (ER) stress response constitutes cellular reactions triggered by a wide variety of stimuli that disturb folding of proteins, often leading to apoptosis. ER stress-induced apoptotic cell death is thought to be an important contributor to many human pathological conditions. The molecular mechanism of this apoptosis process has been highly controversial with both the receptor and the mitochondrial pathways being implicated. Using knockout mouse models and RNAi-mediated gene silencing in cell lines, our group and others had demonstrated the importance of the mitochondrial apoptotic pathway in ER stress-induced cell death, particularly the role of the pro-apoptotic BH3-only BCL-2 family members, BIM and PUMA. However, a recent report suggested a central role for the death receptor, DR5, activated in a ligand-independent manner, and the initiator caspase, caspase-8, in ER stress-induced cell death. This prompted us to re-visit our previous observations and attempt to reproduce the newly published findings. Here we report that the mitochondrial apoptotic pathway, activated by BH3-only proteins, is essential for ER stress-induced cell death and that, in contrast to the previous report, DR5 as well as caspase-8 are not required for this process.
Keywords: Cell Line, Transformed
HCT116 Cells
Endoplasmic Reticulum
Mitochondria
Fibroblasts
Animals
Mice, Knockout
Humans
Mice
Thapsigargin
Brefeldin A
Proto-Oncogene Proteins
Tunicamycin
Signal Transduction
Apoptosis
Gene Expression Regulation
Apoptosis Regulatory Proteins
Caspase 8
Receptors, TNF-Related Apoptosis-Inducing Ligand
Endoplasmic Reticulum Stress
MCF-7 Cells
Bcl-2-Like Protein 11
Rights: © 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved
DOI: 10.1038/cdd.2017.53
Grant ID: http://purl.org/au-research/grants/nhmrc/1085328
Published version: http://dx.doi.org/10.1038/cdd.2017.53
Appears in Collections:Aurora harvest 8
Environment Institute publications

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