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CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3

Jinho Seo, Eun-Woo Lee, Hyerim Sung, Daehyeon Seong, Yves Dondelinger UGent, Jihye Shin, Manhyung Jeong, Hae-Kyung Lee, Jung-Hoon Kim, Su Yeon Han, et al. (2016) NATURE CELL BIOLOGY. 18(3). p.291-302
abstract
Receptor-interacting protein kinase 3 (RIPK3) functions as a key regulator of necroptosis. Here, we report that the RIPK3 expression level is negatively regulated by CHIP (carboxyl terminus of Hsp70-interacting protein; also known as STUB1) E3 ligase-mediated ubiquitylation. Chip(-/-) mouse embryonic fibroblasts and CHIP-depleted L929 and HT-29 cells exhibited higher levels of RIPK3 expression, resulting in increased sensitivity to necroptosis induced by TNF (also known as TNF alpha). These phenomena are due to the CHIP-mediated ubiquitylation of RIPK3, which leads to its lysosomal degradation. Interestingly, RIPK1 expression is also negatively regulated by CHIP-mediated ubiquitylation, validating the major role of CHIP in necrosome formation and sensitivity to TNF-mediated necroptosis. Chip(-/-) mice (C57BL/6) exhibit inflammation in the thymus and massive cell death and disintegration in the small intestinal tract, and die within a few weeks after birth. These phenotypes are rescued by crossing with Ripk3(-/-) mice. These results imply that CHIP is a bona fide negative regulator of the RIPK1-RIPK3 necrosome formation leading to desensitization of TNF-mediated necroptosis.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
CELL-DEATH, DOMAIN-LIKE PROTEIN, MIXED LINEAGE KINASE, PROTEASOMAL DEGRADATION, PROGRAMMED NECROSIS, NLRP3 INFLAMMASOME, TNF-ALPHA, APOPTOSIS, MLKL, UBIQUITINATION
journal title
NATURE CELL BIOLOGY
Nat. Cell Biol.
volume
18
issue
3
pages
291 - 302
Web of Science type
Article
Web of Science id
000371031300010
JCR category
CELL BIOLOGY
JCR impact factor
20.06 (2016)
JCR rank
6/189 (2016)
JCR quartile
1 (2016)
ISSN
1465-7392
DOI
10.1038/ncb3314
language
English
UGent publication?
yes
classification
A1
additional info
the first two authors contributed equally to this work
copyright statement
I have transferred the copyright for this publication to the publisher
id
7162756
handle
http://hdl.handle.net/1854/LU-7162756
date created
2016-03-25 14:39:49
date last changed
2016-12-19 15:47:20
@article{7162756,
  abstract     = {Receptor-interacting protein kinase 3 (RIPK3) functions as a key regulator of necroptosis. Here, we report that the RIPK3 expression level is negatively regulated by CHIP (carboxyl terminus of Hsp70-interacting protein; also known as STUB1) E3 ligase-mediated ubiquitylation. Chip(-/-) mouse embryonic fibroblasts and CHIP-depleted L929 and HT-29 cells exhibited higher levels of RIPK3 expression, resulting in increased sensitivity to necroptosis induced by TNF (also known as TNF alpha). These phenomena are due to the CHIP-mediated ubiquitylation of RIPK3, which leads to its lysosomal degradation. Interestingly, RIPK1 expression is also negatively regulated by CHIP-mediated ubiquitylation, validating the major role of CHIP in necrosome formation and sensitivity to TNF-mediated necroptosis. Chip(-/-) mice (C57BL/6) exhibit inflammation in the thymus and massive cell death and disintegration in the small intestinal tract, and die within a few weeks after birth. These phenotypes are rescued by crossing with Ripk3(-/-) mice. These results imply that CHIP is a bona fide negative regulator of the RIPK1-RIPK3 necrosome formation leading to desensitization of TNF-mediated necroptosis.},
  author       = {Seo, Jinho and Lee, Eun-Woo and Sung, Hyerim and Seong, Daehyeon and Dondelinger, Yves and Shin, Jihye and Jeong, Manhyung and Lee, Hae-Kyung and Kim, Jung-Hoon and Han, Su Yeon and Lee, Cheolju and Seong, Je Kyung and Vandenabeele, Peter and Song, Jaewhan},
  issn         = {1465-7392},
  journal      = {NATURE CELL BIOLOGY},
  keyword      = {CELL-DEATH,DOMAIN-LIKE PROTEIN,MIXED LINEAGE KINASE,PROTEASOMAL DEGRADATION,PROGRAMMED NECROSIS,NLRP3 INFLAMMASOME,TNF-ALPHA,APOPTOSIS,MLKL,UBIQUITINATION},
  language     = {eng},
  number       = {3},
  pages        = {291--302},
  title        = {CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3},
  url          = {http://dx.doi.org/10.1038/ncb3314},
  volume       = {18},
  year         = {2016},
}

Chicago
Seo, Jinho, Eun-Woo Lee, Hyerim Sung, Daehyeon Seong, Yves Dondelinger, Jihye Shin, Manhyung Jeong, et al. 2016. “CHIP Controls Necroptosis Through Ubiquitylation- and Lysosome-dependent Degradation of RIPK3.” Nature Cell Biology 18 (3): 291–302.
APA
Seo, J., Lee, E.-W., Sung, H., Seong, D., Dondelinger, Y., Shin, J., Jeong, M., et al. (2016). CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3. NATURE CELL BIOLOGY, 18(3), 291–302.
Vancouver
1.
Seo J, Lee E-W, Sung H, Seong D, Dondelinger Y, Shin J, et al. CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3. NATURE CELL BIOLOGY. 2016;18(3):291–302.
MLA
Seo, Jinho, Eun-Woo Lee, Hyerim Sung, et al. “CHIP Controls Necroptosis Through Ubiquitylation- and Lysosome-dependent Degradation of RIPK3.” NATURE CELL BIOLOGY 18.3 (2016): 291–302. Print.