Barry Michele, Früh Klaus
Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB T6G 2H7, Canada.
Sci STKE. 2006 May 16;2006(335):pe21. doi: 10.1126/stke.3352006pe21.
Cullin RING ubiquitin ligases (CRULs) are found in all eukaryotes and play an essential role in targeting proteins for ubiquitin-mediated destruction, thus regulating a plethora of cellular processes. Viruses manipulate CRULs by redirecting this destruction machinery to eliminate unwanted host cell proteins, thus allowing viruses to slip past host immune barriers. Depending on the host organism, virus-modified CRULs can perform an amazing range of tasks, including the elimination of crucial signal transduction molecules in the human interferon pathway and suppression of virus-induced gene silencing in plants. This Perspective summarizes recent advances in our understanding of how viral proteins manipulate the function of CRULs.
泛素连接酶(CRULs)存在于所有真核生物中,在将蛋白质靶向泛素介导的降解过程中发挥着重要作用,从而调节众多细胞过程。病毒通过重定向这种降解机制来操控泛素连接酶,以消除不需要的宿主细胞蛋白,从而使病毒能够避开宿主免疫屏障。根据宿主生物体的不同,病毒修饰的泛素连接酶可以执行一系列惊人的任务,包括消除人类干扰素途径中的关键信号转导分子以及抑制植物中病毒诱导的基因沉默。本综述总结了我们在理解病毒蛋白如何操控泛素连接酶功能方面的最新进展。