The Long Form of FLIP Is an Activator of Caspase-8 at the Fas Death-inducing Signaling Complex
Open accessAbstract
Death receptors, such as Fas and tumor necrosis factor-related apoptosis-inducing ligand receptors, recruit Fas-associated death domain and pro-caspase-8 homodimers, which are then autoproteolytically activated. Active caspase-8 is released into the cytoplasm, where it cleaves various proteins including pro-caspase-3, resulting in apoptosis. The cellular Fas-associated death domain-like interleukin-1-beta-converting enzyme-inhibitory protein long form (FLIP(L)), a structural homologue of caspase-8 lacking caspase activity because of several mutations in the active site, is a potent inhibitor of death receptor-induced apoptosis. FLIP(L) is proposed to block caspase-8 activity by forming a proteolytically inactive heterodimer with caspase-8. In contrast, we propose that FLIP(L)-bound caspase-8 is an active protease. Upon heterocomplex formation, a limited caspase-8 autoprocessing occurs resulting in the generation of the p43/41 and the p12 subunits. This partially processed form but also the non-cleaved FLIP(L)-caspase-8 heterocomplex are proteolytically active because they both bind synthetic substrates efficiently. Moreover, FLIP(L) expression favors receptor-interacting kinase (RIP) processing within the Fas-signaling complex. We propose that FLIP(L) inhibits caspase-8 release-dependent pro-apoptotic signals, whereas the single, membrane-restricted active site of the FLIP(L)-caspase-8 heterocomplex is proteolytically active and acts on local substrates such as RIP.
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c-FLIPS inhibits and c-FLIPL activates CASP8 by modulating CASP8 oligomerization.
“Compelling evidence indicates that the short variant of c-FLIP (c-FLIPS) and its long counterpart (c-FLIPL) inhibit and activate CASP8, respectively, by modulating CASP8 oligomerization [298–301].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [300]
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- Authors
- Micheau, O., Thome, M., Schneider, P., Holler, N., Tschopp, J., Nicholson, D. W., Briand, C., & Grütter, M. G.
- Affiliations
- University of Lausanne (CH)
- Merck Canada Inc. (Canada) (CA)
- University of Zurich (CH)
- Corresponding author
- Tschopp, Jürg
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-11
- Volume
- 277
- Issue
- 47
- Pages
- 45162-45171
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2027021865
- Cited by
- 482
- References
- 68
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 9 · 2023: 11 · 2022: 15 · 2021: 7 · 2020: 15 · 2019: 10 · 2018: 12 · 2017: 14 · 2016: 17 · 2015: 22 · 2014: 19 · 2013: 20 · 2012: 21
- FWCI
- 11.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion, other-oa)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- 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 › Inflammasome and immune disorders
- Keywords
- FLIP(L), caspase-8, death receptor signaling, apoptosis, receptor-interacting protein, FADD, caspase-8 inhibition, proteolytic activity
- MeSH terms
- Amino Acid Sequence, Binding Sites, Carrier Proteins, Cell Line, Enzyme Activation, Enzyme Inhibitors, Humans, Ligands, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Signal Transduction, Sequence Alignment, Apoptosis, Protein Structure, Tertiary, fas Receptor, Dimerization, Caspases, Macromolecular Substances, Intracellular Signaling Peptides and Proteins, Cell Size, Caspase 3, Caspase 8, Fas Ligand Protein, CASP8 and FADD-Like Apoptosis Regulating Protein, Caspase 9, Caspase Inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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