Poly-ubiquitination in TNFR1-mediated necroptosis
Open accessAbstract
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.
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Assembly of necrosome upon TNFR1 stimulation impinges on two conditions: pharmacological or genetic CASP8 inactivation, and RIPK1 deubiquitination-dependent phosphorylation (at least in some settings), which can be favored by SMAC mimetics.
“In addition, the assembly of the necrosome upon TNFR1 stimulation impinges on two conditions: (1) pharmacological or genetic CASP8 inactivation [478, 479], and (2) RIPK1 deubiquitination-dependent phosphorylation (at least in some settings), which can be favored by exogenously provided SMAC mimetics, ensuring the release of RIPK1 from complex I (see above) [334, 335, 480, 481].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [480]
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References 104 · Cited by 173
Research works printed but not linked: 1
- [40]Enesa K Zakkar M Chaudhury H le Luong A Rawlinson L Mason JC Haskard DO Dean JL Evans PC NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling J Biol Chem 2008 283 11 7036 7045 10.1074/jbc.M708690200 18178551 · DOI
- Authors
- Dondelinger, Y., Darding, M., Bertrand, M. J. M., & Walczak, H.
- Affiliations
- Ghent University (BE)
- University College London (GB)
- Corresponding author
- Bertrand, Mathieu J. M.
- Walczak, Henning
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2016-04-11
- Volume
- 73
- Issue
- 11-12
- Pages
- 2165-2176
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC4887548
- OpenAlex
- W2333014531
- Cited by
- 173
- References
- 104
- Citations by year
- 2026: 12 · 2025: 13 · 2024: 11 · 2023: 16 · 2022: 25 · 2021: 18 · 2020: 21 · 2019: 16 · 2018: 18 · 2017: 17 · 2016: 6
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Cellular and Molecular Life Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Universiteit Gent
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- polyubiquitination, TNFR1, necroptosis, TNF signaling, complex I, complex II, necrosome, apoptosis, post-translational modification, receptor internalization, inflammatory diseases
- MeSH terms
- Animals, Necrosis, Tumor Necrosis Factor-alpha, Signal Transduction, Apoptosis, Receptors, Tumor Necrosis Factor, Type I, Mice, Receptor-Interacting Protein Serine-Threonine Kinases, Ubiquitination
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