TRIM28 SUMOylates and stabilizes NLRP3 to facilitate inflammasome activation

Ying Qin, Qi Li, Wenbo Liang, Rongzhen Yan, Li Tong, Mutian Jia, Chunyuan Zhao and Wei Zhao ()
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Ying Qin: Shandong University
Qi Li: Shandong University
Wenbo Liang: Shandong University
Rongzhen Yan: Shandong University
Li Tong: Shandong University
Mutian Jia: Shandong University
Chunyuan Zhao: Shandong University
Wei Zhao: Shandong University

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract The cellular NLRP3 protein level is crucial for assembly and activation of the NLRP3 inflammasome. Various posttranslational modifications (PTMs), including phosphorylation and ubiquitination, control NLRP3 protein degradation and inflammasome activation; however, the function of small ubiquitin-like modifier (SUMO) modification (called SUMOylation) in controlling NLRP3 stability and subsequent inflammasome activation is unclear. Here, we show that the E3 SUMO ligase tripartite motif-containing protein 28 (TRIM28) is an enhancer of NLRP3 inflammasome activation by facilitating NLRP3 expression. TRIM28 binds NLRP3, promotes SUMO1, SUMO2 and SUMO3 modification of NLRP3, and thereby inhibits NLRP3 ubiquitination and proteasomal degradation. Concordantly, Trim28 deficiency attenuates NLRP3 inflammasome activation both in vitro and in vivo. These data identify a mechanism by which SUMOylation controls the cellular NLRP3 level and inflammasome activation, and reveal correlations and interactions of NLRP3 SUMOylation and ubiquitination during inflammasome activation.

Date: 2021
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DOI: 10.1038/s41467-021-25033-4

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