Inflammasome activity is controlled by ZBTB16-dependent SUMOylation of ASC

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 () and Dakang Xu ()
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Danfeng Dong: Shanghai Jiao Tong University School of Medicine
Yuzhang Du: Shanghai Jiao Tong University School of Medicine
Xuefeng Fei: Shanghai Jiao Tong University School of Medicine
Hao Yang: Shanghai Jiao Tong University School of Medicine
Xiaofang Li: Northwest Women’s and Children’s Hospital
Xiaobao Yang: Shanghai Jiao Tong University School of Medicine
Junrui Ma: Shanghai Jiao Tong University School of Medicine
Shu Huang: Shanghai Jiao Tong University School of Medicine
Zhihui Ma: Shanghai Jiao Tong University School of Medicine
Juanjuan Zheng: Shanghai Jiao Tong University School of Medicine
David W. Chan: The Chinese University of Hong Kong-Shenzhen
Liyun Shi: Nanjing University of Chinese Medicine
Yunqi Li: Shanghai Jiao Tong University School of Medicine
Aaron T. Irving: Zhejiang University School of Medicine
Xiangliang Yuan: Shanghai Jiao Tong University School of Medicine
Xiangfan Liu: Shanghai Jiao Tong University School of Medicine
Peihua Ni: Shanghai Jiao Tong University School of Medicine
Yiqun Hu: Shanghai Jiao Tong University School of Medicine
Guangxun Meng: University of Chinese Academy of Sciences
Yibing Peng: Shanghai Jiao Tong University School of Medicine
Anthony Sadler: Hudson Institute of Medical Research
Dakang Xu: Shanghai Jiao Tong University School of Medicine

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract 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.

Date: 2023
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DOI: 10.1038/s41467-023-43945-1

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