NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation

	NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation
	Leng, Fangwei 5; Yin, Hang 6; Qin, Siying 6; Zhang, Kai 5; Guan, Yukun 6; Fang, Run 6; Wang, Honglei 1; Li, Guohui 1; Jiang, Zhengfan 6; Sun, Fei 5
刊名	SCIENTIFIC REPORTS
	2020
卷号	10
ISSN号	2045-2322
其他题名	NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation
英文摘要	NOD-like receptors (NLRs) localize in the cytosol to recognize intracellular pathogen products and initialize the innate immune response. However, the ligands and ligand specificity of many NLRs remain unclear. One such NLR, NLRP6, plays an important role in maintaining intestinal homeostasis and protecting against various intestinal diseases such as colitis and intestinal tumorigenesis. Here, we show that the major component of the outer membrane of gram-negative bacteria, lipopolysaccharide (LPS), binds NLRP6 directly and induces global conformational change and dimerization. Following stimulation by ATP, the NLRP6 homodimer can further assemble into a linear molecular platform, and ASC is recruited to form higher molecular structures, indicative of a step-by-step activation mechanism. Our study sheds light on the mystery of LPS-induced inflammasome initiation, reveals the architecture and structural basis of potential pre-inflammasome, and suggests a novel molecular assembly pattern for immune receptors.
资助项目	[National Natural Science Foundation of China] ; [973 National Basic Research Plan of China] ; [Strategic Priority Research Program of the Chinese Academy of Sciences] ; [Chinese Academy of Sciences]
语种	英语
内容类型	期刊论文
源URL	[http://ir.hfcas.ac.cn:8080/handle/334002/124162]
专题	中国科学院合肥物质科学研究院
作者单位	1.Dalian Institute of Chemical Physics, Chinese Academy of Sciences 2.Hefei Institutes of Physical Science, Chinese Academy of Sciences 3.Harvard University 4.Purdue University System 5.Institute of Biophysics, Chinese Academy of Sciences 6.Peking University
推荐引用方式 GB/T 7714	Leng, Fangwei,Yin, Hang,Qin, Siying,et al. NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation[J]. SCIENTIFIC REPORTS,2020,10.
APA	Leng, Fangwei.,Yin, Hang.,Qin, Siying.,Zhang, Kai.,Guan, Yukun.,...&Xie, Can.(2020).NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation.SCIENTIFIC REPORTS,10.
MLA	Leng, Fangwei,et al."NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation".SCIENTIFIC REPORTS 10(2020).