Inflammasome activation controlled by the interplay between post-translational modifications: emerging drug target opportunities
Zhu Liang, Andreas Damianou, Elena Di Daniel, Benedikt M. Kessler
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.
Topics & Concepts
InflammasomeContext (archaeology)UbiquitinCaspase 1KinaseDrug developmentDrug targetSignal transducing adaptor proteinSignal transductionBiologyCell biologyComputational biologyDrugNeuroscienceBioinformaticsInflammationImmunologyPharmacologyBiochemistryGenePaleontologyInflammasome and immune disordersinterferon and immune responsesSphingolipid Metabolism and Signaling