Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non-apoptotic caspase-8 is required for inflammasome priming
Details
Publication Year 2014-07-02,Volume 15,Issue #9,Page 982-990
Journal Title
EMBO Reports
Publication Type
Journal Article
Abstract
A current paradigm proposes that mitochondrial damage is a critical determinant of NLRP3 inflammasome activation. Here, we genetically assess whether mitochondrial signalling represents a unified mechanism to explain how NLRP3 is activated by divergent stimuli. Neither co-deletion of the essential executioners of mitochondrial apoptosis BAK and BAX, nor removal of the mitochondrial permeability transition pore component cyclophilin D, nor loss of the mitophagy regulator Parkin, nor deficiency in MAVS affects NLRP3 inflammasome function. In contrast, caspase-8, a caspase essential for death-receptor-mediated apoptosis, is required for efficient Toll-like-receptor-induced inflammasome priming and cytokine production. Collectively, these results demonstrate that mitochondrial apoptosis is not required for NLRP3 activation, and highlight an important non-apoptotic role for caspase-8 in regulating inflammasome activation and pro-inflammatory cytokine levels.
Publisher
WILEY
Research Division(s)
Cancer And Haematology; Cell Signalling And Cell Death; Chemical Biology; Molecular Genetics Of Cancer; Inflammation
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 2014-07-29 03:01:04
Last Modified: 2015-09-04 11:34:41
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