PHOrming the inflammasome: phosphorylation is a critical switch in inflammasome signalling
Author(s) -
Chloe M McKee,
Fabian A. Fischer,
Jelena S. Bezbradica,
Rebecca C. Coll
Publication year - 2021
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20200987
Subject(s) - inflammasome , phosphorylation , microbiology and biotechnology , signal transducing adaptor protein , innate immune system , aim2 , signalling , inflammation , biology , signal transduction , chemistry , immune system , immunology
Inflammasomes are protein complexes in the innate immune system that regulate the production of pro-inflammatory cytokines and inflammatory cell death. Inflammasome activation and subsequent cell death often occur within minutes to an hour, so the pathway must be dynamically controlled to prevent excessive inflammation and the development of inflammatory diseases. Phosphorylation is a fundamental post-translational modification that allows rapid control over protein function and the phosphorylation of inflammasome proteins has emerged as a key regulatory step in inflammasome activation. Phosphorylation of inflammasome sensor and adapter proteins regulates their inter- and intra-molecular interactions, subcellular localisation, and function. The control of inflammasome phosphorylation may thus provide a new strategy for the development of anti-inflammatory therapeutics. Herein we describe the current knowledge of how phosphorylation operates as a critical switch for inflammasome signalling.
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