Kim Minsoo, Otsubo Ryota, Morikawa Hanako, Nishide Akira, Takagi Kenji, Sasakawa Chihiro, Mizushima Tsunehiro
Division of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku 4-6-1, Tokyo 108-8639, Japan.
Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1, Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Cells. 2014 Aug 18;3(3):848-64. doi: 10.3390/cells3030848.
Protein ubiquitination plays indispensable roles in the regulation of cell homeostasis and pathogenesis of neoplastic, infectious, and neurodegenerative diseases. Given the importance of this modification, it is to be expected that several pathogenic bacteria have developed the ability to utilize the host ubiquitin system for their own benefit. Modulation of the host ubiquitin system by bacterial effector proteins inhibits innate immune responses and hijacks central signaling pathways. Bacterial effectors mimic enzymes of the host ubiquitin system, but may or may not be structurally similar to the mammalian enzymes. Other effectors bind and modify components of the host ubiquitin system, and some are themselves subject to ubiquitination. This review will describe recent findings, based on structural analyses, regarding how pathogens use post-translational modifications of proteins to establish an infection.
蛋白质泛素化在细胞内稳态调节以及肿瘤、感染性和神经退行性疾病的发病机制中发挥着不可或缺的作用。鉴于这种修饰的重要性，可以预期几种致病细菌已发展出利用宿主泛素系统为自身谋利的能力。细菌效应蛋白对宿主泛素系统的调节会抑制先天免疫反应并劫持核心信号通路。细菌效应蛋白模仿宿主泛素系统的酶，但在结构上可能与哺乳动物酶相似，也可能不相似。其他效应蛋白结合并修饰宿主泛素系统的成分，有些自身也会发生泛素化。本综述将基于结构分析描述关于病原体如何利用蛋白质的翻译后修饰来建立感染的最新发现。
