Department of Biochemistry, School of Medicine, Case Western Reserve University Cleveland, OH, USA ; Comprehensive Cancer Center, Case Western Reserve University Cleveland, OH, USA ; University Hospital of Cleveland, Case Western Reserve University Cleveland, OH, USA.
Front Oncol. 2013 Jan 4;2:210. doi: 10.3389/fonc.2012.00210. eCollection 2012.
The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies. Emerging evidences indicated that PML actively participates in many aspects of cellular processes, but the molecular mechanisms underlying PML regulation in response to stress and environmental cues are not complete. Post-translational modifications, such as SUMOylation, phosphorylation, acetylation, and ubiquitination of PML add a complex layer of regulation to the physiological function of PML. In this review, we discuss the fast-moving horizon of post-translational modifications targeting PML.
抑癌蛋白早幼粒细胞白血病蛋白(PML)主要位于一种结构上不同的核内结构域,称为 PML 核体。新出现的证据表明,PML 积极参与细胞过程的许多方面,但 PML 对应激和环境信号的反应的调节的分子机制尚不完全清楚。PML 的翻译后修饰,如 SUMOylation、磷酸化、乙酰化和泛素化,为 PML 的生理功能增加了一个复杂的调控层。在这篇综述中,我们讨论了针对 PML 的翻译后修饰的快速发展领域。