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    Inflammasome activity is important for the immune response and is instrumental in numerous clinical conditions. Here we identify a mechanism that modulates the central Caspase-1 and NLR (Nod-like receptor) adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD). We show that the function of ASC in assembling the inflammasome is controlled by its modification with SUMO (small ubiquitin-like modifier) and identify that the nuclear ZBTB16 (zinc-finger and BTB domain-containing protein 16) promotes this SUMOylation. The physiological significance of this activity is demonstrated through the reduction of acute inflammatory pathogenesis caused by a constitutive hyperactive inflammasome by ablating ZBTB16 in a mouse model of Muckle-Wells syndrome. Together our findings identify an further mechanism by which ZBTB16-dependent control of ASC SUMOylation assembles the inflammasome to promote this pro-inflammatory response. © 2023. The Author(s).

    Citation

    Danfeng Dong, Yuzhang Du, Xuefeng Fei, Hao Yang, Xiaofang Li, Xiaobao Yang, Junrui Ma, Shu Huang, Zhihui Ma, Juanjuan Zheng, David W Chan, Liyun Shi, Yunqi Li, Aaron T Irving, Xiangliang Yuan, Xiangfan Liu, Peihua Ni, Yiqun Hu, Guangxun Meng, Yibing Peng, Anthony Sadler, Dakang Xu. Inflammasome activity is controlled by ZBTB16-dependent SUMOylation of ASC. Nature communications. 2023 Dec 20;14(1):8465

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    PMID: 38123560

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