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Intermediate domain of receptor-interacting protein kinase 1 (RIPK1) determines switch between necroptosis and RIPK1 kinase-dependent apoptosis

Linde Duprez UGent, Mathieu Bertrand UGent, Tom Vanden Berghe UGent, Yves Dondelinger UGent, Nele Festjens UGent and Peter Vandenabeele UGent (2012) JOURNAL OF BIOLOGICAL CHEMISTRY. 287(18). p.14863-14872
abstract
Receptor-interacting protein kinase 1 (RIPK1) is an important component of the tumor necrosis factor receptor 1 (TNFR1) signaling pathway. Depending on the cell type and conditions, RIPK1 mediates MAPK and NF-kappa B activation as well as cell death. Using a mutant form of RIPK1 (RIPK1 Delta ID) lacking the intermediate domain (ID), we confirm the requirement of this domain for activation of these signaling events. Moreover, expression of RIPK1 Delta ID resulted in enhanced recruitment of caspase-8 to the TNFR1 complex II component Fas-associated death domain (FADD), which allowed a shift from TNF-induced necroptosis to apoptosis in L929 cells. Addition of the RIPK1 kinase inhibitor necrostatin-1 strongly reduced recruitment of RIPK1 and caspase-8 to FADD and subsequent apoptosis, indicating a role for RIPK1 kinase activity in apoptotic complex formation. Our study shows that RIPK1 has an anti-apoptotic function residing in its ID and demonstrates a cellular system as an elegant genetic model for RIPK1 kinase-dependent apoptosis that, in contrast to the Smac mimetic model, does not rely on depletion of cellular inhibitor of apoptosis protein 1 and 2 (cIAP1/2).
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
NF-KAPPA-B, SIGNALING COMPLEX, MECHANISMS, TUMOR-NECROSIS-FACTOR, NONAPOPTOTIC CELL-DEATH, TNF-ALPHA, L929 CELLS, ACTIVATION, UBIQUITINATION, CIAP1
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
287
issue
18
pages
14863 - 14872
Web of Science type
Article
Web of Science id
000304003200050
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
4.651 (2012)
JCR rank
61/288 (2012)
JCR quartile
1 (2012)
ISSN
0021-9258
DOI
10.1074/jbc.M111.288670
project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
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
2153307
handle
http://hdl.handle.net/1854/LU-2153307
date created
2012-06-14 11:55:18
date last changed
2014-05-12 11:00:26
@article{2153307,
  abstract     = {Receptor-interacting protein kinase 1 (RIPK1) is an important component of the tumor necrosis factor receptor 1 (TNFR1) signaling pathway. Depending on the cell type and conditions, RIPK1 mediates MAPK and NF-kappa B activation as well as cell death. Using a mutant form of RIPK1 (RIPK1 Delta ID) lacking the intermediate domain (ID), we confirm the requirement of this domain for activation of these signaling events. Moreover, expression of RIPK1 Delta ID resulted in enhanced recruitment of caspase-8 to the TNFR1 complex II component Fas-associated death domain (FADD), which allowed a shift from TNF-induced necroptosis to apoptosis in L929 cells. Addition of the RIPK1 kinase inhibitor necrostatin-1 strongly reduced recruitment of RIPK1 and caspase-8 to FADD and subsequent apoptosis, indicating a role for RIPK1 kinase activity in apoptotic complex formation. Our study shows that RIPK1 has an anti-apoptotic function residing in its ID and demonstrates a cellular system as an elegant genetic model for RIPK1 kinase-dependent apoptosis that, in contrast to the Smac mimetic model, does not rely on depletion of cellular inhibitor of apoptosis protein 1 and 2 (cIAP1/2).},
  author       = {Duprez, Linde and Bertrand, Mathieu and Vanden Berghe, Tom and Dondelinger, Yves and Festjens, Nele and Vandenabeele, Peter},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {NF-KAPPA-B,SIGNALING COMPLEX,MECHANISMS,TUMOR-NECROSIS-FACTOR,NONAPOPTOTIC CELL-DEATH,TNF-ALPHA,L929 CELLS,ACTIVATION,UBIQUITINATION,CIAP1},
  language     = {eng},
  number       = {18},
  pages        = {14863--14872},
  title        = {Intermediate domain of receptor-interacting protein kinase 1 (RIPK1) determines switch between necroptosis and RIPK1 kinase-dependent apoptosis},
  url          = {http://dx.doi.org/10.1074/jbc.M111.288670},
  volume       = {287},
  year         = {2012},
}

Chicago
Duprez, Linde, Mathieu Bertrand, Tom Vanden Berghe, Yves Dondelinger, Nele Festjens, and Peter Vandenabeele. 2012. “Intermediate Domain of Receptor-interacting Protein Kinase 1 (RIPK1) Determines Switch Between Necroptosis and RIPK1 Kinase-dependent Apoptosis.” Journal of Biological Chemistry 287 (18): 14863–14872.
APA
Duprez, Linde, Bertrand, M., Vanden Berghe, T., Dondelinger, Y., Festjens, N., & Vandenabeele, P. (2012). Intermediate domain of receptor-interacting protein kinase 1 (RIPK1) determines switch between necroptosis and RIPK1 kinase-dependent apoptosis. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(18), 14863–14872.
Vancouver
1.
Duprez L, Bertrand M, Vanden Berghe T, Dondelinger Y, Festjens N, Vandenabeele P. Intermediate domain of receptor-interacting protein kinase 1 (RIPK1) determines switch between necroptosis and RIPK1 kinase-dependent apoptosis. JOURNAL OF BIOLOGICAL CHEMISTRY. 2012;287(18):14863–72.
MLA
Duprez, Linde, Mathieu Bertrand, Tom Vanden Berghe, et al. “Intermediate Domain of Receptor-interacting Protein Kinase 1 (RIPK1) Determines Switch Between Necroptosis and RIPK1 Kinase-dependent Apoptosis.” JOURNAL OF BIOLOGICAL CHEMISTRY 287.18 (2012): 14863–14872. Print.