ZBP1 promotes LPS-induced cell death and IL-1β release via RHIM-mediated interactions with RIPK1
| Autor: | Vladimir Ilyukha, Avishekh Gautam, Alexei Degterev, Wilson M. Connolly, Zoie Magri, Alexander Poltorak, Irina Smirnova, Hayley I. Muendlein |
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| Rok vydání: | 2021 |
| Předmět: |
Lipopolysaccharides
0301 basic medicine Programmed cell death Science Interleukin-1beta General Physics and Astronomy Context (language use) Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences RIPK1 0302 clinical medicine Cell death and immune response medicine Animals Yersinia pseudotuberculosis FADD Caspase 8 Multidisciplinary Cell Death biology Effector Chemistry Immune cell death RNA-Binding Proteins Inflammasome General Chemistry biology.organism_classification Yersinia Toll-like receptors Cell biology Mice Inbred C57BL Adaptor Proteins Vesicular Transport 030104 developmental biology Receptors Tumor Necrosis Factor Type I TRIF Receptor-Interacting Protein Serine-Threonine Kinases biology.protein Infection 030217 neurology & neurosurgery Protein Binding medicine.drug |
| Zdroj: | Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Inflammation and cell death are closely linked arms of the host immune response to infection, which when carefully balanced ensure host survival. One example of this balance is the tightly regulated transition from TNFR1-associated pro-inflammatory complex I to pro-death complex II. By contrast, here we show that a TRIF-dependent complex containing FADD, RIPK1 and caspase-8 (that we have termed the TRIFosome) mediates cell death in response to Yersinia pseudotuberculosis and LPS. Furthermore, we show that constitutive binding between ZBP1 and RIPK1 is essential for the initiation of TRIFosome interactions, caspase-8-mediated cell death and inflammasome activation, thus positioning ZBP1 as an effector of cell death in the context of bacterial blockade of pro-inflammatory signaling. Additionally, our findings offer an alternative to the TNFR1-dependent model of complex II assembly, by demonstrating pro-death complex formation reliant on TRIF signaling. Yersiania YopJ protein has been shown to drive caspase-8-mediated pyroptosis. Here the authors show a precise mechanism of this non-canonical cell death pathway that is controlled by a TRIF-dependent complex of FADD, RIPK1, caspase-8 and ZBP1. |
| Databáze: | OpenAIRE |
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