Centre d'étude d'agents Pathogènes et Biotechnologies pour la Santé (CPBS-CNRS), Montpellier Cedex 5, France.
Biol Cell. 2012 Mar;104(3):165-87. doi: 10.1111/boc.201100112. Epub 2012 Jan 23.
The modification of intracellular proteins by ubiquitin (Ub) and ubiquitin-like (UbL) proteins is a central mechanism for regulating and fine-tuning all cellular processes. Indeed, these modifications are widely used to control the stability, activity and localisation of many key proteins and, therefore, they are instrumental in regulating cellular functions as diverse as protein degradation, cell signalling, vesicle trafficking and immune response. It is thus no surprise that pathogens in general, and viruses in particular, have developed multiple strategies to either counteract or exploit the complex mechanisms mediated by the Ub and UbL protein conjugation pathways. The aim of this review is to provide an overview on the intricate and conflicting relationships that intimately link HIV-1 and these sophisticated systems of post-translational modifications.
泛素（Ub）和类泛素（UbL）蛋白对细胞内蛋白的修饰是调节和微调所有细胞过程的核心机制。事实上，这些修饰被广泛用于控制许多关键蛋白的稳定性、活性和定位，因此，它们在调节细胞功能方面起着重要作用，如蛋白降解、细胞信号转导、囊泡运输和免疫反应。因此，病原体，尤其是病毒，已经开发出多种策略来对抗或利用 Ub 和 UbL 蛋白缀合途径介导的复杂机制，这并不奇怪。本综述的目的是概述 HIV-1 与这些复杂的翻译后修饰系统之间复杂而又相互矛盾的关系。
