Inflammasome activation controlled by the interplay between post-translational modifications: emerging drug target opportunities

Journal article

AbstractControlling 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.

Authors: Liang, Z; Damianou, A; Di Daniel, E; Kessler, BM

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: BioMed Central
• Journal: Cell Communication and Signaling
• Volume: 19
• Issue: 1
• Pages: 23-23
• Article number: 23
• Publication date: 2021-02-24
• DOI: 10.1186/s12964-020-00688-6
• EISSN: 1478-811X
• ISSN: 1478-811X
• Language: English
• Keywords: Inflammasome; Neuroscience; Ubiquitin; Immunology; Drug target; Cell biology; Biochemistry; Biology; Pharmacology; Caspase 1; Computational biology; Context (archaeology); Signal transduction; Signal transducing adaptor protein; Drug; Inflammation; Bioinformatics; Kinase; Drug development