Posttranslational Regulation of Inflammasomes, Its Potential as Biomarkers and in the Identification of Novel Drugs Targets

In this review, we have summarized classical post-translational modifications (PTMs) such as phosphorylation, ubiquitylation, and SUMOylation of the different components of one of the most studied NLRP3, and other emerging inflammasomes. We will highlight how the discovery of these modifications have provided mechanistic insight into the biology, function, and regulation of these multiprotein complexes not only in the context of the innate immune system but also in adaptive immunity, hematopoiesis, bone marrow transplantation, as well and their role in human diseases. We have also collected available information concerning less-studied modifications such as acetylation, ADP-ribosylation, nitrosylation, prenylation, citrullination, and emphasized their relevance in the regulation of inflammasome complex formation. We have described disease-associated mutations affecting PTMs of inflammasome components. Finally, we have discussed how a deeper understanding of different PTMs can help the development of biomarkers and identification of novel drug targets to treat diseases caused by the malfunctioning of inflammasomes.

Automated summary

This review summarizes classical post-translational modifications (PTMs) such as phosphorylation, ubiquitylation, and SUMOylation of the different components of NLRP3 and other emerging inflammasomes. The importance of these modifications in the biology, function, and regulation of these multiprotein complexes in various immune processes and human diseases is highlighted. Less-studied modifications and disease-associated mutations affecting PTMs are also discussed. The review concludes by emphasizing how a deeper understanding of different PTMs can contribute to the development of biomarkers and identification of novel drug targets for diseases associated with inflammasome malfunctioning.