Université de Bourgogne Franche-Comté, LNC UMR1231, 21000 Dijon, France.
Institut National de la Santé et de la Recherche Médicale (Inserm), LNC UMR1231, 21000 Dijon, France.
Int J Mol Sci. 2017 Oct 19;18(10):2188. doi: 10.3390/ijms18102188.
Ubiquitination is a post-translational modification that defines the cellular fate of intracellular proteins. It can modify their stability, their activity, their subcellular location, and even their interacting pattern. This modification is a reversible event whose implementation is easy and fast. It contributes to the rapid adaptation of the cells to physiological intracellular variations and to intracellular or environmental stresses. E2F1 (E2 promoter binding factor 1) transcription factor is a potent cell cycle regulator. It displays contradictory functions able to regulate both cell proliferation and cell death. Its expression and activity are tightly regulated over the course of the cell cycle progression and in response to genotoxic stress. I discuss here the most recent evidence demonstrating the role of ubiquitination in E2F1's regulation.
泛素化是一种翻译后修饰,它决定了细胞内蛋白质的命运。它可以修饰它们的稳定性、活性、亚细胞位置,甚至它们的相互作用模式。这种修饰是一个容易且快速实现的可逆事件。它有助于细胞快速适应生理细胞内变化和细胞内或环境压力。E2F1(E2 启动子结合因子 1)转录因子是一种有效的细胞周期调节剂。它具有相反的功能,既能调节细胞增殖,又能调节细胞死亡。其表达和活性在细胞周期进展过程中以及对遗传毒性应激的反应中受到严格调控。本文讨论了最近的证据,证明了泛素化在 E2F1 调控中的作用。