RIP3 mediates the embryonic lethality of caspase-8-deficient mice

William J. Kaiser (), Jason W. Upton, Alyssa B. Long, Devon Livingston-Rosanoff, Lisa P. Daley-Bauer, Razqallah Hakem, Tamara Caspary and Edward S. Mocarski
Additional contact information
William J. Kaiser: Emory Vaccine Center, Emory University School of Medicine
Jason W. Upton: Emory Vaccine Center, Emory University School of Medicine
Alyssa B. Long: Emory University
Devon Livingston-Rosanoff: Emory Vaccine Center, Emory University School of Medicine
Lisa P. Daley-Bauer: Emory Vaccine Center, Emory University School of Medicine
Razqallah Hakem: University of Toronto and Ontario Cancer Institute, University Health Network
Tamara Caspary: Emory University
Edward S. Mocarski: Emory Vaccine Center, Emory University School of Medicine

Nature, 2011, vol. 471, issue 7338, 368-372

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/nature09857

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