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FADD and Caspase-8 Mediate Priming and Activation of the Canonical and Noncanonical Nlrp3 Inflammasomes
Author(s) -
Prajwal Gurung,
Paras Anand,
R. K. Subbarao Malireddi,
Lieselotte Vande Walle,
Nina Van Opdenbosch,
Christopher P. Dillon,
Ricardo Weinlich,
Douglas R. Green,
Mohamed Lamkanfi,
ThirumalaDevi Kanneganti
Publication year - 2014
Publication title -
the journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.1302839
Subject(s) - fadd , inflammasome , aim2 , caspase 8 , nlrc4 , microbiology and biotechnology , caspase 1 , priming (agriculture) , caspase , chemistry , nlrp1 , biology , apoptosis , biochemistry , receptor , programmed cell death , botany , germination
The Nlrp3 inflammasome is critical for host immunity, but the mechanisms controlling its activation are enigmatic. In this study, we show that loss of FADD or caspase-8 in a RIP3-deficient background, but not RIP3 deficiency alone, hampered transcriptional priming and posttranslational activation of the canonical and noncanonical Nlrp3 inflammasome. Deletion of caspase-8 in the presence or absence of RIP3 inhibited caspase-1 and caspase-11 activation by Nlrp3 stimuli but not the Nlrc4 inflammasome. In addition, FADD deletion prevented caspase-8 maturation, positioning FADD upstream of caspase-8. Consequently, FADD- and caspase-8-deficient mice had impaired IL-1β production when challenged with LPS or infected with the enteropathogen Citrobacter rodentium. Thus, our results reveal FADD and caspase-8 as apical mediators of canonical and noncanonical Nlrp3 inflammasome priming and activation.

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