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

Andrew Oberst, Christopher P. Dillon, Ricardo Weinlich, Laura L. McCormick, Patrick Fitzgerald, Cristina Pop, Razq Hakem, Guy S. Salvesen and Douglas R. Green ()
Additional contact information
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

Nature, 2011, vol. 471, issue 7338, 363-367

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.

Date: 2011
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DOI: 10.1038/nature09852

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