Flipping the Switch from Inflammation to Cell Death

Multiple research groups have demonstrated that caspase-8 (CASP8)-mediated gasdermin D (GSDMD) cleavage drives pyroptotic cell death. Here, we discuss a novel role for the enzymatically inactive homolog of CASP8, the long isoform of cellular FLICE-like inhibitory protein (cFLIPL), in the regulation...

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Bibliographic Details
Published in:Trends in immunology 2020-08, Vol.41 (8), p.648-651
Main Authors: Muendlein, Hayley I., Poltorak, Alexander
Format: Article
Language:English
Subjects:
Animals
Apoptosis
Bacterial infections
c-FLIP protein
CASP8 and FADD-Like Apoptosis Regulating Protein - deficiency
Caspase 8 - metabolism
Caspase-8
Cell activation
Cell death
Genotype & phenotype
Homology
Humans
Infections
Inflammation
Inflammation - pathology
Kinases
Models, Immunological
Mortality
Proteins
Pyroptosis
Signal Transduction - immunology
Tumor necrosis factor-TNF
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Description
Summary:Multiple research groups have demonstrated that caspase-8 (CASP8)-mediated gasdermin D (GSDMD) cleavage drives pyroptotic cell death. Here, we discuss a novel role for the enzymatically inactive homolog of CASP8, the long isoform of cellular FLICE-like inhibitory protein (cFLIPL), in the regulation of this process. Specifically, cFLIP-deficiency provides a model in which to study the mechanisms regulating CASP8-mediated activation of cell death and inflammatory signaling.
ISSN:1471-4906
1471-4981
DOI:10.1016/j.it.2020.06.007