Ghent University Academic Bibliography

Advanced

cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)

Mathieu Bertrand UGent, Saskia Lippens UGent, An Staes UGent, Barbara Gilbert UGent, Ria Roelandt UGent, Jelle De Medts UGent, Kris Gevaert UGent, Wim Declercq UGent and Peter Vandenabeele UGent (2011) PLOS ONE. 6(9).
abstract
The RIP kinases have emerged as essential mediators of cellular stress that integrate both extracellular stimuli emanating from various cell-surface receptors and signals coming from intracellular pattern recognition receptors. The molecular mechanisms regulating the ability of the RIP proteins to transduce the stress signals remain poorly understood, but seem to rely only partially on their kinase activities. Recent studies on RIP1 and RIP2 have highlighted the importance of ubiquitination as a key process regulating their capacity to activate downstream signaling pathways. In this study, we found that XIAP, cIAP1 and cIAP2 not only directly bind to RIP1 and RIP2 but also to RIP3 and RIP4. We show that cIAP1 and cIAP2 are direct E3 ubiquitin ligases for all four RIP proteins and that cIAP1 is capable of conjugating the RIPs with diverse types of ubiquitin chains, including linear chains. Consistently, we show that repressing cIAP1/2 levels affects the activation of NF-kappa B that is dependent on RIP1, -2, -3 and -4. Finally, we identified Lys51 and Lys145 of RIP4 as two critical residues for cIAP1-mediated ubiquitination and NF-kB activation.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
C-ASSOCIATED KINASE, NF-KAPPA-B, TNF-ALPHA, SIGNALING COMPLEX, ACTIVATION, C-IAP1, NECROSIS, IMMUNE-RESPONSES, APOPTOSIS PROTEINS, CELL-DEATH
journal title
PLOS ONE
PLoS One
volume
6
issue
9
article_number
e22356
pages
11 pages
Web of Science type
Article
Web of Science id
000294803200001
JCR category
BIOLOGY
JCR impact factor
4.092 (2011)
JCR rank
12/84 (2011)
JCR quartile
1 (2011)
ISSN
1932-6203
DOI
10.1371/journal.pone.0022356
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
1917686
handle
http://hdl.handle.net/1854/LU-1917686
date created
2011-09-29 13:44:10
date last changed
2013-02-27 09:08:14
@article{1917686,
  abstract     = {The RIP kinases have emerged as essential mediators of cellular stress that integrate both extracellular stimuli emanating from various cell-surface receptors and signals coming from intracellular pattern recognition receptors. The molecular mechanisms regulating the ability of the RIP proteins to transduce the stress signals remain poorly understood, but seem to rely only partially on their kinase activities. Recent studies on RIP1 and RIP2 have highlighted the importance of ubiquitination as a key process regulating their capacity to activate downstream signaling pathways. In this study, we found that XIAP, cIAP1 and cIAP2 not only directly bind to RIP1 and RIP2 but also to RIP3 and RIP4. We show that cIAP1 and cIAP2 are direct E3 ubiquitin ligases for all four RIP proteins and that cIAP1 is capable of conjugating the RIPs with diverse types of ubiquitin chains, including linear chains. Consistently, we show that repressing cIAP1/2 levels affects the activation of NF-kappa B that is dependent on RIP1, -2, -3 and -4. Finally, we identified Lys51 and Lys145 of RIP4 as two critical residues for cIAP1-mediated ubiquitination and NF-kB activation.},
  articleno    = {e22356},
  author       = {Bertrand, Mathieu and Lippens, Saskia and Staes, An and Gilbert, Barbara and Roelandt, Ria and De Medts, Jelle and Gevaert, Kris and Declercq, Wim and Vandenabeele, Peter},
  issn         = {1932-6203},
  journal      = {PLOS ONE},
  keyword      = {C-ASSOCIATED KINASE,NF-KAPPA-B,TNF-ALPHA,SIGNALING COMPLEX,ACTIVATION,C-IAP1,NECROSIS,IMMUNE-RESPONSES,APOPTOSIS PROTEINS,CELL-DEATH},
  language     = {eng},
  number       = {9},
  pages        = {11},
  title        = {cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)},
  url          = {http://dx.doi.org/10.1371/journal.pone.0022356},
  volume       = {6},
  year         = {2011},
}

Chicago
Bertrand, Mathieu, Saskia Lippens, An Staes, Barbara Gilbert, Ria Roelandt, Jelle De Medts, Kris Gevaert, Wim Declercq, and Peter Vandenabeele. 2011. “cIAP1/2 Are Direct E3 Ligases Conjugating Diverse Types of Ubiquitin Chains to Receptor Interacting Proteins Kinases 1 to 4 (RIP1-4).” Plos One 6 (9).
APA
Bertrand, M., Lippens, S., Staes, A., Gilbert, B., Roelandt, R., De Medts, J., Gevaert, K., et al. (2011). cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4). PLOS ONE, 6(9).
Vancouver
1.
Bertrand M, Lippens S, Staes A, Gilbert B, Roelandt R, De Medts J, et al. cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4). PLOS ONE. 2011;6(9).
MLA
Bertrand, Mathieu, Saskia Lippens, An Staes, et al. “cIAP1/2 Are Direct E3 Ligases Conjugating Diverse Types of Ubiquitin Chains to Receptor Interacting Proteins Kinases 1 to 4 (RIP1-4).” PLOS ONE 6.9 (2011): n. pag. Print.