| Literature DB >> 33627128 |
Zhu Liang1,2, Andreas Damianou3, Elena Di Daniel3,4, Benedikt M Kessler5,6.
Abstract
Controlling the activation of the NLRP3 inflammasome by post-translational modifications (PTMs) of critical protein subunits has emerged as a key determinant in inflammatory processes as well as in pathophysiology. In this review, we put into context the kinases, ubiquitin processing and other PTM enzymes that modify NLRP3, ASC/PYCARD and caspase-1, leading to inflammasome regulation, activation and signal termination. Potential target therapeutic entry points for a number of inflammatory diseases focussed on PTM enzyme readers, writers and erasers, leading to the regulation of inflammasome function, are discussed. Video Abstract.Entities:
Keywords: Drug targets; NLRP3 inflammasome; Post-translational modifications; Protein interaction; Signalling
Mesh:
Substances:
Year: 2021 PMID: 33627128 PMCID: PMC7905589 DOI: 10.1186/s12964-020-00688-6
Source DB: PubMed Journal: Cell Commun Signal ISSN: 1478-811X Impact factor: 5.712