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

被引：29
|
作者：
Liang, Zhu [1 ,3 ]
Damianou, Andreas [1 ]
Di Daniel, Elena [1 ,2 ]
Kessler, Benedikt M. [1 ,3 ]
机构：
[1] Univ Oxford, Target Discovery Inst, Ctr Med Discovery, Nuffield Dept Med, Oxford OX3 7FZ, England
[2] Univ Oxford, ARUK Oxford Drug Discovery Inst, Nuffield Dept Med, Oxford OX3 7FZ, England
[3] Chinese Acad Med Sci, Univ Oxford, Nuffield Dept Med, CAMS Oxford Inst, Oxford OX3 7FZ, England
来源：
CELL COMMUNICATION AND SIGNALING | 2021年 / 19卷 / 01期
关键词：
NLRP3; inflammasome; Post-translational modifications; Protein interaction; Signalling; Drug targets; BRUTONS TYROSINE KINASE; NLRP3; INFLAMMASOME; CASPASE-1; ACTIVATION; ASC; PHOSPHORYLATION; INHIBITION; DEUBIQUITINATION; UBIQUITINATION; CONTRIBUTES; MUTATIONS;
D O I：
10.1186/s12964-020-00688-6
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
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.
引用
收藏
页数：12
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