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TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members

Nele Vanlangenakker UGent, Mathieu Bertrand UGent, Pieter Bogaert UGent, Peter Vandenabeele UGent and Tom Vanden Berghe UGent (2011) CELL DEATH & DISEASE. 2.
abstract
TNF receptor 1 signaling induces NF-kappa B activation and necroptosis in L929 cells. We previously reported that cellular inhibitor of apoptosis protein-mediated receptor-interacting protein 1 (RIP1) ubiquitination acts as a cytoprotective mechanism, whereas knockdown of cylindromatosis, a RIP1-deubiquitinating enzyme, protects against tumor necrosis factor (TNF)-induced necroptosis. We report here that RIP1 is a crucial mediator of canonical NF-kappa B activation in L929 cells, therefore questioning the relative cytoprotective contribution of RIP1 ubiquitination versus canonical NF-kappa B activation. We found that attenuated NF-kappa B activation has no impact on TNF-induced necroptosis. However, we identified A20 and linear ubiquitin chain assembly complex as negative regulators of necroptosis. Unexpectedly, and in contrast to RIP3, we also found that knockdown of RIP1 did not block TNF cytotoxicity. Cell death typing revealed that RIP1-depleted cells switch from necroptotic to apoptotic death, indicating that RIP1 can also suppress apoptosis in L929 cells. Inversely, we observed that Fas-associated protein via a death domain, cellular FLICE inhibitory protein and caspase-8, which are all involved in the initiation of apoptosis, counteract necroptosis induction. Finally, we also report RIP1-independent but RIP3-mediated necroptosis in the context of TNF signaling in particular conditions.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
RIP1, TNF-induced necroptosis, A20, LUBAC, TUMOR-NECROSIS-FACTOR, NF-KAPPA-B, DEATH DOMAIN KINASE, SIGNALING COMPLEX, INDUCED APOPTOSIS, FACTOR RECEPTOR-1, ACTIVATION, ALPHA, RIP1, UBIQUITINATION
journal title
CELL DEATH & DISEASE
Cell Death Dis.
volume
2
article_number
e230
pages
10 pages
Web of Science type
Article
Web of Science id
000297688600008
JCR category
CELL BIOLOGY
JCR impact factor
5.333 (2011)
JCR rank
45/178 (2011)
JCR quartile
2 (2011)
ISSN
2041-4889
DOI
10.1038/cddis.2011.111
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
1996578
handle
http://hdl.handle.net/1854/LU-1996578
date created
2012-01-19 13:26:42
date last changed
2013-02-27 09:09:26
@article{1996578,
  abstract     = {TNF receptor 1 signaling induces NF-kappa B activation and necroptosis in L929 cells. We previously reported that cellular inhibitor of apoptosis protein-mediated receptor-interacting protein 1 (RIP1) ubiquitination acts as a cytoprotective mechanism, whereas knockdown of cylindromatosis, a RIP1-deubiquitinating enzyme, protects against tumor necrosis factor (TNF)-induced necroptosis. We report here that RIP1 is a crucial mediator of canonical NF-kappa B activation in L929 cells, therefore questioning the relative cytoprotective contribution of RIP1 ubiquitination versus canonical NF-kappa B activation. We found that attenuated NF-kappa B activation has no impact on TNF-induced necroptosis. However, we identified A20 and linear ubiquitin chain assembly complex as negative regulators of necroptosis. Unexpectedly, and in contrast to RIP3, we also found that knockdown of RIP1 did not block TNF cytotoxicity. Cell death typing revealed that RIP1-depleted cells switch from necroptotic to apoptotic death, indicating that RIP1 can also suppress apoptosis in L929 cells. Inversely, we observed that Fas-associated protein via a death domain, cellular FLICE inhibitory protein and caspase-8, which are all involved in the initiation of apoptosis, counteract necroptosis induction. Finally, we also report RIP1-independent but RIP3-mediated necroptosis in the context of TNF signaling in particular conditions.},
  articleno    = {e230},
  author       = {Vanlangenakker, Nele and Bertrand, Mathieu and Bogaert, Pieter and Vandenabeele, Peter and Vanden Berghe, Tom},
  issn         = {2041-4889},
  journal      = {CELL DEATH \& DISEASE},
  keyword      = {RIP1,TNF-induced necroptosis,A20,LUBAC,TUMOR-NECROSIS-FACTOR,NF-KAPPA-B,DEATH DOMAIN KINASE,SIGNALING COMPLEX,INDUCED APOPTOSIS,FACTOR RECEPTOR-1,ACTIVATION,ALPHA,RIP1,UBIQUITINATION},
  language     = {eng},
  pages        = {10},
  title        = {TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members},
  url          = {http://dx.doi.org/10.1038/cddis.2011.111},
  volume       = {2},
  year         = {2011},
}

Chicago
Vanlangenakker, Nele, Mathieu Bertrand, Pieter Bogaert, Peter Vandenabeele, and Tom Vanden Berghe. 2011. “TNF-induced Necroptosis in L929 Cells Is Tightly Regulated by Multiple TNFR1 Complex I and II Members.” Cell Death & Disease 2.
APA
Vanlangenakker, N., Bertrand, M., Bogaert, P., Vandenabeele, P., & Vanden Berghe, T. (2011). TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members. CELL DEATH & DISEASE, 2.
Vancouver
1.
Vanlangenakker N, Bertrand M, Bogaert P, Vandenabeele P, Vanden Berghe T. TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members. CELL DEATH & DISEASE. 2011;2.
MLA
Vanlangenakker, Nele, Mathieu Bertrand, Pieter Bogaert, et al. “TNF-induced Necroptosis in L929 Cells Is Tightly Regulated by Multiple TNFR1 Complex I and II Members.” CELL DEATH & DISEASE 2 (2011): n. pag. Print.