期刊
SCIENCE
卷 362, 期 6418, 页码 1064-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aau2818
关键词
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资金
- National Institutes of Health [AI07538, AI129527, AI067497, AI083713, AI095213, AI139914, AI075118, HL092610]
- Norwegian Cancer Society [7699133, B05035/001]
- UMass Medical School Summer Undergraduate Research Experience Program
- Research Council of Norway Center of Excellence [223255/F50]
Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via inflammasome-activated caspase-1 or -11. It is currently unknown whether macrophage GSDMD can be processed by other mechanisms. Here, we describe an additional pathway controlling GSDMD processing. The inhibition of TAK1 or I kappa B kinase (IKK) by the Yersinia effector protein YopJ elicits RIPK1- and caspase-8-dependent cleavage of GSDMD, which subsequently results in cell death. GSDMD processing also contributes to the NLRP3 inflammasome-dependent release of interleukin-1 beta (IL-1 beta). Thus, caspase-8 acts as a regulator of GSDMD-driven cell death. Furthermore, this study establishes the importance of TAK1 and IKK activity in the control of GSDMD cleavage and cytotoxicity.
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