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Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappa B pathway

Antoine Tinel, Sophie Janssens UGent, Saskia Lippens UGent, Solange Cuenin, Emmanuelle Logette, Bastienne Jaccard, Manfredo Quadroni and Juerg Tschopp (2007) EMBO JOURNAL. 26(1). p.197-208
abstract
Upon DNA damage, a complex called the PIDDosome is formed and either signals NF-kappa B activation and thus cell survival or alternatively triggers caspase-2 activation and apoptosis. PIDD (p53-induced protein with a death domain) is constitutively processed giving rise to a 48-kDa N-terminal fragment containing the leucine-rich repeats (LRRs, PIDD-N) and a 51-kDa C-terminal fragment containing the death domain (DD, PIDD-C). The latter undergoes further cleavage resulting in a 37-kDa fragment (PIDD-CC). Here we show that processing occurs at S446 (generating PIDD-C) and S588 (generating PIDD-CC) by an auto-processing mechanism similar to that found in the nuclear pore protein Nup98/ 96 and inteins. Auto-cleavage of PIDD determines the outcome of the downstream signaling events. Whereas initially formed PIDD-C mediates the activation of NF-kappa B via the recruitment of RIP-1 and NEMO, subsequent formation of PIDD-CC causes caspase-2 activation and thus cell death. A non-cleavable PIDD mutant is unable to translocate from the cytoplasm to the nucleus and loses both activities. In this way, autoproteolysis of PIDD might participate in the orchestration of the DNA damage-induced life and death signaling pathways.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
DNA-DAMAGE, DOMAIN-CONTAINING PROTEIN, INDUCED APOPTOSIS, COUPLED RECEPTOR, GENOTOXIC STRESS, ACTIVATION, NUCLEOPORIN, CLEAVAGE, MOTIF, P53, auto-proteolysis, caspase-2, DNA damage, NF-kappa B, PIDD
journal title
EMBO JOURNAL
Embo J.
volume
26
issue
1
pages
197 - 208
Web of Science type
Article
Web of Science id
000243730600018
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
8.662 (2007)
JCR rank
19/260 (2007)
JCR quartile
1 (2007)
ISSN
0261-4189
DOI
10.1038/sj.emboj.7601473
language
English
UGent publication?
no
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1202553
handle
http://hdl.handle.net/1854/LU-1202553
date created
2011-04-05 13:16:15
date last changed
2016-12-19 15:45:49
@article{1202553,
  abstract     = {Upon DNA damage, a complex called the PIDDosome is formed and either signals NF-kappa B activation and thus cell survival or alternatively triggers caspase-2 activation and apoptosis. PIDD (p53-induced protein with a death domain) is constitutively processed giving rise to a 48-kDa N-terminal fragment containing the leucine-rich repeats (LRRs, PIDD-N) and a 51-kDa C-terminal fragment containing the death domain (DD, PIDD-C). The latter undergoes further cleavage resulting in a 37-kDa fragment (PIDD-CC). Here we show that processing occurs at S446 (generating PIDD-C) and S588 (generating PIDD-CC) by an auto-processing mechanism similar to that found in the nuclear pore protein Nup98/ 96 and inteins. Auto-cleavage of PIDD determines the outcome of the downstream signaling events. Whereas initially formed PIDD-C mediates the activation of NF-kappa B via the recruitment of RIP-1 and NEMO, subsequent formation of PIDD-CC causes caspase-2 activation and thus cell death. A non-cleavable PIDD mutant is unable to translocate from the cytoplasm to the nucleus and loses both activities. In this way, autoproteolysis of PIDD might participate in the orchestration of the DNA damage-induced life and death signaling pathways.},
  author       = {Tinel, Antoine and Janssens, Sophie and Lippens, Saskia and Cuenin, Solange and Logette, Emmanuelle and Jaccard, Bastienne and Quadroni, Manfredo and Tschopp, Juerg},
  issn         = {0261-4189},
  journal      = {EMBO JOURNAL},
  keyword      = {DNA-DAMAGE,DOMAIN-CONTAINING PROTEIN,INDUCED APOPTOSIS,COUPLED RECEPTOR,GENOTOXIC STRESS,ACTIVATION,NUCLEOPORIN,CLEAVAGE,MOTIF,P53,auto-proteolysis,caspase-2,DNA damage,NF-kappa B,PIDD},
  language     = {eng},
  number       = {1},
  pages        = {197--208},
  title        = {Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappa B pathway},
  url          = {http://dx.doi.org/10.1038/sj.emboj.7601473},
  volume       = {26},
  year         = {2007},
}

Chicago
Tinel, Antoine, Sophie Janssens, Saskia Lippens, Solange Cuenin, Emmanuelle Logette, Bastienne Jaccard, Manfredo Quadroni, and Juerg Tschopp. 2007. “Autoproteolysis of PIDD Marks the Bifurcation Between Pro-death Caspase-2 and Pro-survival NF-kappa B Pathway.” Embo Journal 26 (1): 197–208.
APA
Tinel, Antoine, Janssens, S., Lippens, S., Cuenin, S., Logette, E., Jaccard, B., Quadroni, M., et al. (2007). Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappa B pathway. EMBO JOURNAL, 26(1), 197–208.
Vancouver
1.
Tinel A, Janssens S, Lippens S, Cuenin S, Logette E, Jaccard B, et al. Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappa B pathway. EMBO JOURNAL. 2007;26(1):197–208.
MLA
Tinel, Antoine, Sophie Janssens, Saskia Lippens, et al. “Autoproteolysis of PIDD Marks the Bifurcation Between Pro-death Caspase-2 and Pro-survival NF-kappa B Pathway.” EMBO JOURNAL 26.1 (2007): 197–208. Print.