Literature DB >> 34854899

PHOrming the inflammasome: phosphorylation is a critical switch in inflammasome signalling.

Chloe M McKee1, Fabian A Fischer2, Jelena S Bezbradica2, Rebecca C Coll1.   

Abstract

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.
© 2021 The Author(s).

Entities:  

Keywords:  NLRP3; inflammasome; inflammation; phosphorylation/dephosphorylation; post translational modification

Mesh:

Substances:

Year:  2021        PMID: 34854899      PMCID: PMC8786285          DOI: 10.1042/BST20200987

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  99 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  2016-11-22       Impact factor: 11.205

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