Journal
CELL DEATH & DISEASE
Volume 10, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41419-019-1847-z
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Funding
- Science Foundation Ireland
- Irish Government
- Health Research Board [HRA-POR-2014-643]
- Science Foundation Ireland (SFI) grant under the European Regional Development Fund [13/RC/2073]
- SFI Starting Investigator Grant [15/SIRG/3528]
- Canada Research Chairs program
- Irish Research Council Fellowship [EBPPG/2014/74]
- European Commission [Horizon 2020 Collaborative Health Project NEPHSTROM] [634086]
- European Commission [FP7 Collaborative Health Project VISICORT] [602470]
- Science Foundation Ireland [REMEDI Strategic Research Cluster] [09/SRC-B1794]
- CURAM Research Centre [13/RC/2073]
- Molecular Medicine Ireland Clinical and Translational Research Scholarship - Irish Government's Programme for Research in Third Level Institutions, Cycle5
- College of Medicine, Nursing and Health Sciences of the National University of Ireland Galway
- NUI Galway
- Science Foundation Ireland (SFI) [15/SIRG/3528] Funding Source: Science Foundation Ireland (SFI)
- Irish Research Council (IRC) [EBPPG/2014/74] Funding Source: Irish Research Council (IRC)
- Health Research Board (HRB) [HRA-POR-2014-643] Funding Source: Health Research Board (HRB)
- H2020 Societal Challenges Programme [634086] Funding Source: H2020 Societal Challenges Programme
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The inflammasome is a multiprotein complex assembled in response to Pathogen Associated Molecular Patterns (PAMPs) and Danger Associated Molecular Patterns (DAMPS). Inflammasome activation occurs through a two-step mechanism, with the first signal facilitating priming of inflammasome components while the second signal triggers complex assembly. Once assembled, the inflammasome recruits and activates pro-caspase-1, which in turn processes pro-interleukin (IL)-18 and pro-IL-1 beta into their bio-active forms. Owing to its key role in the regulation of innate immune responses, the inflammasome has emerged as a therapeutic target for the treatment of inflammatory conditions. In this study we demonstrate that IRE1 alpha, a key component of the Unfolded Protein Response, contributes to assembly of the NLRP3 inflammasome. Blockade of IRE1 alpha RNase signaling lowered NLRP3 inflammasome assembly, caspase-1 activation and pro-IL-1 beta processing. These results underscore both the importance and potential therapeutic relevance of targeting IRE1 alpha signaling in conditions of excessive inflammasome formation.
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