Behuliak M, Celec P, Gardlik R, Palffy R
BiomeD research & publishing group, Department of Molecular Biology, Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia.
Bratisl Lek Listy. 2005;106(3):93-100.
The Nobel prize in chemistry 2004 was given to Aaron Ciechanover, Avram Hershko and Irwin Rose for their discovery of the ubiquitin mediated proteolysis. Years of research have shown that the ubiquitin pathway plays a crucial role in the cellular metabolism and its regulation. These scientists together with Alexander Varshavsky have identified the most important elements of this pathway as well as their interactions. The ubiquitin pathway degrades intracellular proteins with an ubiquitin chain being the tag that marks proteins assigned for degradation. This process is mediated by ubiquitin-activating enzyme (El), ubiquitin-conjugating enzymes (E2) and ubiquitin-protein ligases (E3). Mono-ubiquitination and deubiquitination play a classic regulatory role in numerous processes including cell-cycle, transcription, translation, DNA repair, stress response etc. This article tries to summarize current knowledge on the molecular basis of the ubiqutin pathway. (Fig. 1, Ref. 52.)
2004年诺贝尔化学奖授予阿龙·切哈诺沃、阿夫拉姆·赫什科和欧文·罗斯，以表彰他们发现了泛素介导的蛋白质水解过程。多年的研究表明，泛素途径在细胞代谢及其调节中起着至关重要的作用。这些科学家与亚历山大·瓦尔沙夫斯基一起确定了该途径的最重要元素及其相互作用。泛素途径通过泛素链降解细胞内蛋白质，泛素链是标记待降解蛋白质的标签。这个过程由泛素激活酶（E1）、泛素结合酶（E2）和泛素-蛋白连接酶（E3）介导。单泛素化和去泛素化在包括细胞周期、转录、翻译、DNA修复、应激反应等众多过程中发挥着经典的调节作用。本文试图总结关于泛素途径分子基础的当前知识。（图1，参考文献52）
