Poly-ubiquitination in TNFR1-mediated necroptosis
- Author
- Yves Dondelinger (UGent) , Maurice Darding, Mathieu Bertrand (UGent) and Henning Walczak
- Organization
- Abstract
- Tumor necrosis factor (TNF) is a master pro-inflammatory cytokine, and inappropriate TNF signaling is implicated in the pathology of many inflammatory diseases. Ligation of TNF to its receptor TNFR1 induces the transient formation of a primary membrane-bound signaling complex, known as complex I, that drives expression of pro-survival genes. Defective complex I activation results in induction of cell death, in the form of apoptosis or necroptosis. This switch occurs via internalization of complex I components and assembly and activation of secondary cytoplasmic death complexes, respectively known as complex II and necrosome. In this review, we discuss the crucial regulatory functions of ubiquitination-a post-translational protein modification consisting of the covalent attachment of ubiquitin, and multiples thereof, to target proteins-to the various steps of TNFR1 signaling leading to necroptosis.
- Keywords
- NF-KAPPA-B, TUMOR-NECROSIS-FACTOR, CHRONIC PROLIFERATIVE DERMATITIS, SIGNAL-INDUCED PHOSPHORYLATION, RECEPTOR INTERACTING PROTEIN, LINEAR, POLYUBIQUITIN CHAINS, TNF-INDUCED NECROSIS, CELL-DEATH, DEUBIQUITINATING, ENZYME, PROGRAMMED NECROSIS, Ubiquitination, Necroptosis, TNFR1, RIPK1, c IAP1/2, LUBAC, A20, CYLD
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8522266
- MLA
- Dondelinger, Yves, et al. “Poly-Ubiquitination in TNFR1-Mediated Necroptosis.” CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 73, no. 11–12, 2016, pp. 2165–76, doi:10.1007/s00018-016-2191-4.
- APA
- Dondelinger, Y., Darding, M., Bertrand, M., & Walczak, H. (2016). Poly-ubiquitination in TNFR1-mediated necroptosis. CELLULAR AND MOLECULAR LIFE SCIENCES, 73(11–12), 2165–2176. https://doi.org/10.1007/s00018-016-2191-4
- Chicago author-date
- Dondelinger, Yves, Maurice Darding, Mathieu Bertrand, and Henning Walczak. 2016. “Poly-Ubiquitination in TNFR1-Mediated Necroptosis.” CELLULAR AND MOLECULAR LIFE SCIENCES 73 (11–12): 2165–76. https://doi.org/10.1007/s00018-016-2191-4.
- Chicago author-date (all authors)
- Dondelinger, Yves, Maurice Darding, Mathieu Bertrand, and Henning Walczak. 2016. “Poly-Ubiquitination in TNFR1-Mediated Necroptosis.” CELLULAR AND MOLECULAR LIFE SCIENCES 73 (11–12): 2165–2176. doi:10.1007/s00018-016-2191-4.
- Vancouver
- 1.Dondelinger Y, Darding M, Bertrand M, Walczak H. Poly-ubiquitination in TNFR1-mediated necroptosis. CELLULAR AND MOLECULAR LIFE SCIENCES. 2016;73(11–12):2165–76.
- IEEE
- [1]Y. Dondelinger, M. Darding, M. Bertrand, and H. Walczak, “Poly-ubiquitination in TNFR1-mediated necroptosis,” CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 73, no. 11–12, pp. 2165–2176, 2016.
@article{8522266,
abstract = {{Tumor necrosis factor (TNF) is a master pro-inflammatory cytokine, and inappropriate TNF signaling is implicated in the pathology of many inflammatory diseases. Ligation of TNF to its receptor TNFR1 induces the transient formation of a primary membrane-bound signaling complex, known as complex I, that drives expression of pro-survival genes. Defective complex I activation results in induction of cell death, in the form of apoptosis or necroptosis. This switch occurs via internalization of complex I components and assembly and activation of secondary cytoplasmic death complexes, respectively known as complex II and necrosome. In this review, we discuss the crucial regulatory functions of ubiquitination-a post-translational protein modification consisting of the covalent attachment of ubiquitin, and multiples thereof, to target proteins-to the various steps of TNFR1 signaling leading to necroptosis.}},
author = {{Dondelinger, Yves and Darding, Maurice and Bertrand, Mathieu and Walczak, Henning}},
issn = {{1420-682X}},
journal = {{CELLULAR AND MOLECULAR LIFE SCIENCES}},
keywords = {{NF-KAPPA-B,TUMOR-NECROSIS-FACTOR,CHRONIC PROLIFERATIVE DERMATITIS,SIGNAL-INDUCED PHOSPHORYLATION,RECEPTOR INTERACTING PROTEIN,LINEAR,POLYUBIQUITIN CHAINS,TNF-INDUCED NECROSIS,CELL-DEATH,DEUBIQUITINATING,ENZYME,PROGRAMMED NECROSIS,Ubiquitination,Necroptosis,TNFR1,RIPK1,c IAP1/2,LUBAC,A20,CYLD}},
language = {{eng}},
number = {{11-12}},
pages = {{2165--2176}},
title = {{Poly-ubiquitination in TNFR1-mediated necroptosis}},
url = {{http://dx.doi.org/10.1007/s00018-016-2191-4}},
volume = {{73}},
year = {{2016}},
}
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