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cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

Nele Vanlangenakker UGent, Tom Vanden Berghe UGent, Pieter Bogaert UGent, Bram Laukens UGent, K Zobel, K Deshayes, D Vucic, S Fulda, Peter Vandenabeele UGent and Mathieu Bertrand UGent (2011) CELL DEATH AND DIFFERENTIATION. 18(4). p.656-665
abstract
Three members of the IAP family (X-linked inhibitor of apoptosis (XIAP), cellular inhibitor of apoptosis proteins-1/-2 (cIAP1 and cIAP2)) are potent suppressors of apoptosis. Recent studies have shown that cIAP1 and cIAP2, unlike XIAP, are not direct caspase inhibitors, but block apoptosis by functioning as E3 ligases for effector caspases and receptor-interacting protein 1 (RIP1). cIAP-mediated polyubiquitination of RIP1 allows it to bind to the pro-survival kinase transforming growth factor-beta-activated kinase 1 (TAK1) which prevents it from activating caspase-8-dependent death, a process reverted by the deubiquitinase CYLD. RIP1 is also a regulator of necrosis, a caspase-independent type of cell death. Here, we show that cells depleted of the IAPs by treatment with the IAP antagonist BV6 are greatly sensitized to tumor necrosis factor (TNF)-induced necrosis, but not to necrotic death induced by anti-Fas, poly(I:C) oxidative stress. Specific targeting of the IAPs by RNAi revealed that repression of cIAP1 is responsible for the sensitization. Similarly, lowering TAK1 levels or inhibiting its kinase activity sensitized cells to TNF-induced necrosis, whereas repressing CYLD had the opposite effect. We show that this sensitization to death is accompanied by enhanced RIP1 kinase activity, increased recruitment of RIP1 to Fas-associated via death domain and RIP3 (which allows necrosome formation), and elevated RIP1 kinase-dependent accumulation of reactive oxygen species (ROS). In conclusion, our data indicate that cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent ROS production. Cell Death and Differentiation (2011) 18, 656-665; doi:10.1038/cdd.2010.138; published online 5 November 2010
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
KAPPA-B ACTIVATION, MOLECULAR-MECHANISMS, ALPHA-DEPENDENT APOPTOSIS, necrosome, DOMAIN KINASE RIP, RECEPTOR-INTERACTING PROTEIN, cIAP1, TAK1, smac mimetic, necrosis, TNFR1, NADPH OXIDASE, DEATH, INHIBITOR, C-IAP2, UBIQUITINATION
journal title
CELL DEATH AND DIFFERENTIATION
Cell Death Differ.
volume
18
issue
4
pages
656 - 665
Web of Science type
Article
Web of Science id
000288314800008
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
8.849 (2011)
JCR rank
23/286 (2011)
JCR quartile
1 (2011)
ISSN
1350-9047
DOI
10.1038/cdd.2010.138
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1197972
handle
http://hdl.handle.net/1854/LU-1197972
date created
2011-03-28 14:06:08
date last changed
2013-02-27 09:09:22
@article{1197972,
  abstract     = {Three members of the IAP family (X-linked inhibitor of apoptosis (XIAP), cellular inhibitor of apoptosis proteins-1/-2 (cIAP1 and cIAP2)) are potent suppressors of apoptosis. Recent studies have shown that cIAP1 and cIAP2, unlike XIAP, are not direct caspase inhibitors, but block apoptosis by functioning as E3 ligases for effector caspases and receptor-interacting protein 1 (RIP1). cIAP-mediated polyubiquitination of RIP1 allows it to bind to the pro-survival kinase transforming growth factor-beta-activated kinase 1 (TAK1) which prevents it from activating caspase-8-dependent death, a process reverted by the deubiquitinase CYLD. RIP1 is also a regulator of necrosis, a caspase-independent type of cell death. Here, we show that cells depleted of the IAPs by treatment with the IAP antagonist BV6 are greatly sensitized to tumor necrosis factor (TNF)-induced necrosis, but not to necrotic death induced by anti-Fas, poly(I:C) oxidative stress. Specific targeting of the IAPs by RNAi revealed that repression of cIAP1 is responsible for the sensitization. Similarly, lowering TAK1 levels or inhibiting its kinase activity sensitized cells to TNF-induced necrosis, whereas repressing CYLD had the opposite effect. We show that this sensitization to death is accompanied by enhanced RIP1 kinase activity, increased recruitment of RIP1 to Fas-associated via death domain and RIP3 (which allows necrosome formation), and elevated RIP1 kinase-dependent accumulation of reactive oxygen species (ROS). In conclusion, our data indicate that cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent ROS production. Cell Death and Differentiation (2011) 18, 656-665; doi:10.1038/cdd.2010.138; published online 5 November 2010},
  author       = {Vanlangenakker, Nele and Vanden Berghe, Tom and Bogaert, Pieter and Laukens, Bram and Zobel, K and Deshayes, K and Vucic, D and Fulda, S and Vandenabeele, Peter and Bertrand, Mathieu},
  issn         = {1350-9047},
  journal      = {CELL DEATH AND DIFFERENTIATION},
  keyword      = {KAPPA-B ACTIVATION,MOLECULAR-MECHANISMS,ALPHA-DEPENDENT APOPTOSIS,necrosome,DOMAIN KINASE RIP,RECEPTOR-INTERACTING PROTEIN,cIAP1,TAK1,smac mimetic,necrosis,TNFR1,NADPH OXIDASE,DEATH,INHIBITOR,C-IAP2,UBIQUITINATION},
  language     = {eng},
  number       = {4},
  pages        = {656--665},
  title        = {cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production},
  url          = {http://dx.doi.org/10.1038/cdd.2010.138},
  volume       = {18},
  year         = {2011},
}

Chicago
Vanlangenakker, Nele, Tom Vanden Berghe, Pieter Bogaert, Bram Laukens, K Zobel, K Deshayes, D Vucic, S Fulda, Peter Vandenabeele, and Mathieu Bertrand. 2011. “cIAP1 and TAK1 Protect Cells from TNF-induced Necrosis by Preventing RIP1/RIP3-dependent Reactive Oxygen Species Production.” Cell Death and Differentiation 18 (4): 656–665.
APA
Vanlangenakker, N., Vanden Berghe, T., Bogaert, P., Laukens, B., Zobel, K., Deshayes, K., Vucic, D., et al. (2011). cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. CELL DEATH AND DIFFERENTIATION, 18(4), 656–665.
Vancouver
1.
Vanlangenakker N, Vanden Berghe T, Bogaert P, Laukens B, Zobel K, Deshayes K, et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. CELL DEATH AND DIFFERENTIATION. 2011;18(4):656–65.
MLA
Vanlangenakker, Nele, Tom Vanden Berghe, Pieter Bogaert, et al. “cIAP1 and TAK1 Protect Cells from TNF-induced Necrosis by Preventing RIP1/RIP3-dependent Reactive Oxygen Species Production.” CELL DEATH AND DIFFERENTIATION 18.4 (2011): 656–665. Print.