RIKEN Plant Science Center, Suehiro-cho 1-7-22 Tsurumi-ku, Yokohama 230-0045, Japan.
Trends Biochem Sci. 2010 Apr;35(4):199-207. doi: 10.1016/j.tibs.2009.12.005. Epub 2010 Jan 22.
The NLR (nucleotide-binding domain and leucine-rich repeat containing) proteins provide pathogen-sensing systems that are conserved in both plants and animals. They can be activated directly or indirectly by pathogen-derived molecules through mechanisms that remain largely elusive. Studies in plants revealed that the molecular chaperone, HSP90, and its co-chaperones, SGT1 and RAR1, are major stabilizing factors for NLR proteins. More recent work indicates that SGT1 and HSP90 are also required for the function of NLR proteins in mammals, underscoring the evolutionary conservation of innate immune system regulatory mechanisms. Comparative analyses of plant and mammalian NLR proteins, together with recent insights provided by the structure of SGT1-HSP90 complex, have begun to uncover the mechanisms by which immune NLR sensors are regulated.
NLR（核苷酸结合域和富含亮氨酸重复序列）蛋白提供了病原体感应系统，该系统在植物和动物中都保守。它们可以通过机制直接或间接被病原体衍生的分子激活，这些机制在很大程度上仍然难以捉摸。在植物中的研究表明，分子伴侣 HSP90 及其共伴侣 SGT1 和 RAR1 是 NLR 蛋白的主要稳定因子。最近的研究表明，SGT1 和 HSP90 也需要在哺乳动物中 NLR 蛋白的功能，突出了先天免疫系统调节机制的进化保守性。植物和哺乳动物 NLR 蛋白的比较分析，以及 SGT1-HSP90 复合物结构提供的最新见解，已经开始揭示免疫 NLR 传感器的调节机制。
