The linear ubiquitin chain assembly complex regulates TRAIL‐induced gene activation and cell death
Open accessAbstract
The linear ubiquitin chain assembly complex (LUBAC) is the only known E3 ubiquitin ligase which catalyses the generation of linear ubiquitin linkages de novo . LUBAC is a crucial component of various immune receptor signalling pathways. Here, we show that LUBAC forms part of the TRAIL‐R‐associated complex I as well as of the cytoplasmic TRAIL‐induced complex II. In both of these complexes, HOIP limits caspase‐8 activity and, consequently, apoptosis whilst being itself cleaved in a caspase‐8‐dependent manner. Yet, by limiting the formation of a RIPK1/RIPK3/MLKL‐containing complex, LUBAC also restricts TRAIL‐induced necroptosis. We identify RIPK1 and caspase‐8 as linearly ubiquitinated targets of LUBAC following TRAIL stimulation. Contrary to its role in preventing TRAIL‐induced RIPK1‐independent apoptosis, HOIP presence, but not its activity, is required for preventing necroptosis. By promoting recruitment of the IKK complex to complex I, LUBAC also promotes TRAIL‐induced activation of NF‐κB and, consequently, the production of cytokines, downstream of FADD, caspase‐8 and cIAP1/2. Hence, LUBAC controls the TRAIL signalling outcome from complex I and II, two platforms which both trigger cell death and gene activation.
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Upon TRAILR activation, LUBAC ubiquitinates both CASP8 and RIPK1 while promoting recruitment of IKK to complex I.
“Upon TRAILR activation, LUBAC reportedly ubiquitinates both CASP8 and RIPK1 while promoting the recruitment of IKK to complex I [286]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [286]
Ability of some death receptors including TNFR1 to promote NF-κB activation over CASP8 activation depends on degree of receptor oligomerization, scaffolding functions of CASP8, and assembly of TNFR1-like complexes containing RIPK1 and LUBAC.
“The ability of some death receptors including TNFR1 to promote NF-κB activation over CASP8 activation appears to depend on the degree of receptor oligomerization (i.e., trimerization vs. higher-order multimerization) [343], the scaffolding (i.e., non-enzymatic) functions of CASP8, and the consequent assembly of TNFR1-like complexes containing RIPK1 and LUBAC [272, 286, 344].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [286]
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Advances in the Structural and Physiological Functions of SHARPIN
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Mechanisms underlying linear ubiquitination and implications in tumorigenesis and drug discovery
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Benedetto, C. D., Khan, T., Serrano-Saenz, S., Rodriguez-Lemus, A., Klomsiri, C., Beutel, T.-M., Thach, A., Walczak, H., & Betancur, P. A. (2023) · Cancers · doi:10.3390/cancers15030967 · Cited by 3 · see citing works
Self-citationFocus on necroptosis: its role in the pathogenesis and therapeutic potential of osteoarthritis
Ouyang, Y., Liao, H., Kang, W., Li, F., & Shen, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1695254 · Cited by 1 · see citing works
- Authors
- Lafont, E., Kantari‐Mimoun, C., Draber, P., De Miguel, D., Hartwig, T., Reichert, M., Kupka, S., Shimizu, Y., Taraborrelli, L., Spit, M., Sprick, M. R., & Walczak, H.
- Affiliations
- University College London (GB)
- Heidelberg Institute for Stem Cell Technology and Experimental Medicine (DE)
- Corresponding author
- Walczak, Henning
- Venue
- The EMBO Journal
- Published
- 2017-03-03
- Volume
- 36
- Issue
- 9
- Pages
- 1147-1166
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC5412822
- OpenAlex
- W2594607272
- Cited by
- 114
- References
- 95
- Citations by year
- 2026: 8 · 2025: 5 · 2024: 13 · 2023: 11 · 2022: 13 · 2021: 8 · 2020: 15 · 2019: 18 · 2018: 14 · 2017: 9
- FWCI
- 6.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- The EMBO Journal (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome (096831/Z/11/Z)
- European Research Council (294880)
- Cancer Research UK (A17341, 515818, 525877)
- Biotechnology and Biological Sciences Research Council (BB/J013129/1)
- KWF Kankerbestrijding (BUIT 2015‐7526)
- 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 › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- LUBAC, HOIP, caspase-8, RIPK1, RIPK3, MLKL, necroptosis, apoptosis, linear ubiquitination, NF-κB activation, IKK complex, FADD, cIAP1/2, cytokine production, gene activation
- MeSH terms
- Cell Line, Humans, Transcriptional Activation, Cell Death, Ubiquitin-Protein Ligases, Receptors, TNF-Related Apoptosis-Inducing Ligand, TNF-Related Apoptosis-Inducing Ligand
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