Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity

Lu, Jennifer V.; Weist, Brian M.; van Raam, Bram J.; Marro, Brett S.; Nguyen, Long V.; Srinivas, Prathna; Bell, Bryan D.; Luhrs, Keith A.; Lane, Thomas E.; Salvesen, Guy S.; Walsh, Craig M.

doi:10.1073/pnas.1102779108

Cited by 123Cell death mechanisms and regulationT-cell and B-cell ImmunologyNF-κB Signaling Pathways

Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity

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Lu, Jennifer V., Weist, Brian M., van Raam, Bram J., Marro, Brett S., Nguyen, Long V., Srinivas, Prathna, Bell, Bryan D., Luhrs, Keith A. +3 more·2011·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1102779108PMC PMC3174674

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Abstract

Caspase-8 (casp8) is required for extrinsic apoptosis, and mice deficient in casp8 fail to develop and die in utero while ultimately failing to maintain the proliferation of T cells, B cells, and a host of other cell types. Paradoxically, these failures are not caused by a defect in apoptosis, but by a presumed proliferative function of this protease. Indeed, following mitogenic stimulation, T cells lacking casp8 or its adaptor protein FADD (Fas-associated death domain protein) develop a hyperautophagic morphology, and die a programmed necrosis-like death process termed necroptosis. Recent studies have demonstrated that receptor-interacting protein kinases (RIPKs) RIPK1 and RIPK3 together facilitate TNF-induced necroptosis, but the precise role of RIPKs in the demise of T cells lacking FADD or casp8 activity is unknown. Here we demonstrate that RIPK3 and FADD have opposing and complementary roles in promoting T-cell clonal expansion and homeostasis. We show that the defective proliferation of T cells bearing an interfering form of FADD (FADDdd) is rescued by crossing with RIPK3 −/− mice, although such rescue ultimately leads to lymphadenopathy. Enhanced recovery of these double-mutant T cells following stimulation demonstrates that FADD, casp8, and RIPK3 are all essential for clonal expansion, contraction, and antiviral responses. Finally, we demonstrate that caspase-mediated cleavage of RIPK1-containing necrosis inducing complexes (necrosomes) is sufficient to prevent necroptosis in the face of death receptor signaling. These studies highlight the “two-faced” nature of casp8 activity, promoting clonal expansion in some situations and apoptotic demise in others.

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Proliferative defects of Casp8−/− or Fadd−/− T cells can be rescued by administration of RIPK1 inhibitor Nec-1 or concomitant ablation of Ripk3.
“Moreover, the proliferative defects of Casp8−/− or Fadd−/− T cells can be rescued by the administration of the RIPK1 inhibitor Nec-1 or the concomitant ablation of Ripk3 [489].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [489]

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Authors: Lu, J. V., Weist, B. M., van Raam, B. J., Marro, B. S., Nguyen, L. V., Srinivas, P., Bell, B. D., Luhrs, K. A., Lane, T. E., Salvesen, G. S., & Walsh, C. M.
Affiliations: University of California, Irvine (US)
Sanford–Burnham Medical Research Institute, La Jolla, CA 92037
Sanford Burnham Prebys Medical Discovery Institute (US)
ORCID: Weist, Brian M.
Marro, Brett S.
Lane, Thomas E.
Salvesen, Guy S.
Walsh, Craig M.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2011-08-29
Volume: 108
Issue: 37
Pages: 15312-15317
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1102779108
PMC: PMC3174674
OpenAlex: W2089868528
Cited by: 122
References: 40
Citations by year: 2026: 1 · 2025: 2 · 2024: 6 · 2023: 4 · 2022: 4 · 2021: 4 · 2020: 10 · 2019: 10 · 2018: 6 · 2017: 5 · 2016: 13 · 2015: 17 · 2014: 14 · 2013: 10 · 2012: 11
FWCI: 5.07
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (CA 69381, P01CA069381, P30CA062203, T32CA009054)
National Institute of Allergy and Infectious Diseases (R01AI063419, AI50506, R01AI050506, AI63419)
National Institute of Neurological Disorders and Stroke (NS41249, R01NS041249)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: FADD, RIPK3, caspase-8, T cell homeostasis, T cell clonal expansion, necroptosis, necrosome, RIPK1, antiviral immunity, death receptor signaling, apoptosis, lymphadenopathy, T cell proliferation
MeSH terms: Animals, Cell Survival, Crosses, Genetic, Female, Murine hepatitis virus, Hepatitis, Viral, Animal, Homeostasis, Immunity, Male, CD8-Positive T-Lymphocytes, Cell Proliferation, Mice, Fas-Associated Death Domain Protein, Receptor-Interacting Protein Serine-Threonine Kinases

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Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity

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