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Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis

Author

Listed:
  • Andrew Oberst

    (Dept. of Immunology, St. Jude Children’s Research Hospital)

  • Christopher P. Dillon

    (Dept. of Immunology, St. Jude Children’s Research Hospital)

  • Ricardo Weinlich

    (Dept. of Immunology, St. Jude Children’s Research Hospital)

  • Laura L. McCormick

    (Dept. of Immunology, St. Jude Children’s Research Hospital)

  • Patrick Fitzgerald

    (Dept. of Immunology, St. Jude Children’s Research Hospital)

  • Cristina Pop

    (Program in Apoptosis and Cell Death Research, Sanford-Burnham Medical Research Institute)

  • Razq Hakem

    (Ontario Cancer Institute, University of Toronto)

  • Guy S. Salvesen

    (Program in Apoptosis and Cell Death Research, Sanford-Burnham Medical Research Institute)

  • Douglas R. Green

    (Dept. of Immunology, St. Jude Children’s Research Hospital)

Abstract

Caspase-8 joins RIPK at the death Caspase-8 mediates apoptosis induced by 'death receptors' on the cell's surface. At the same time, it is able to prevent receptor interacting protein kinase (RIPK)-dependent necrosis. Without caspase-8, mice die during embryonic development, but why this happens is not clear. Two groups show that this lethality is not caused by the absence of apoptosis, but by the RIPK3-dependent necrosis that is unleashed without caspase-8. Mice lacking both caspase-8 and RIP3 develop into viable, immunocompetent adults, but have a progressive lymphoaccumulative disease similar to that in mice that lack the CD95 death receptor. Oberst et al. also show that caspase-8 forms a proteolytically active complex with FLICE-like inhibitory protein long (FLIPL), and that this complex is required for protection against RIP3-dependent necrosis.

Suggested Citation

  • Andrew Oberst & Christopher P. Dillon & Ricardo Weinlich & Laura L. McCormick & Patrick Fitzgerald & Cristina Pop & Razq Hakem & Guy S. Salvesen & Douglas R. Green, 2011. "Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis," Nature, Nature, vol. 471(7338), pages 363-367, March.
    • Handle: RePEc:nat:nature:v:471:y:2011:i:7338:d:10.1038_nature09852
    DOI: 10.1038/nature09852
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    Cited by:

    1. Maria C. Tanzer & Isabell Bludau & Che A. Stafford & Veit Hornung & Matthias Mann, 2021. "Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. Joo-Hui Han & Rajendra Karki & R. K. Subbarao Malireddi & Raghvendra Mall & Roman Sarkar & Bhesh Raj Sharma & Jonathon Klein & Harmut Berns & Harshan Pisharath & Shondra M. Pruett-Miller & Sung-Jin Ba, 2024. "NINJ1 mediates inflammatory cell death, PANoptosis, and lethality during infection conditions and heat stress," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Chao-Yu Yang & Yi-Chun Tseng & Yi-Fan Tu & Bai-Jiun Kuo & Li-Chung Hsu & Chia-I Lien & You-Sheng Lin & Yin-Ting Wang & Yen-Chen Lu & Tsung-Wei Su & Yu-Chih Lo & Su-Chang Lin, 2024. "Reverse hierarchical DED assembly in the cFLIP-procaspase-8 and cFLIP-procaspase-8-FADD complexes," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    4. Chao-Yu Yang & Chia-I Lien & Yi-Chun Tseng & Yi-Fan Tu & Arkadiusz W. Kulczyk & Yen-Chen Lu & Yin-Ting Wang & Tsung-Wei Su & Li-Chung Hsu & Yu-Chih Lo & Su-Chang Lin, 2024. "Deciphering DED assembly mechanisms in FADD-procaspase-8-cFLIP complexes regulating apoptosis," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    5. Esther Hoste & Kim Lecomte & Karl Annusver & Niels Vandamme & Jana Roels & Sophia Maschalidi & Lien Verboom & Hanna-Kaisa Vikkula & Mozes Sze & Lisette Van Hove & Kevin Verstaen & Arne Martens & Tino , 2021. "OTULIN maintains skin homeostasis by controlling keratinocyte death and stem cell identity," Nature Communications, Nature, vol. 12(1), pages 1-16, December.

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