Wang Jianlin, Qiu Zhaoping, Wu Yadi
Department of Pharmacology & Nutritional Sciences, University of Kentucky School of Medicine, KY 40506, USA.
Markey Cancer Center, University of Kentucky School of Medicine, Lexington, KY 40506, USA.
Cells. 2018 Aug 27;7(9):118. doi: 10.3390/cells7090118.
Histone post-translational modifications influence many fundamental cellular events by regulating chromatin structure and gene transcriptional activity. These modifications are highly dynamic and tightly controlled, with many enzymes devoted to the addition and removal of these modifications. Interestingly, these modifying enzymes are themselves fine-tuned and precisely regulated at the level of protein turnover by ubiquitin-proteasomal processing. Here, we focus on recent progress centered on the mechanisms regulating ubiquitination of histone modifying enzymes, including ubiquitin proteasomal degradation and the reverse process of deubiquitination. We will also discuss the potential pathophysiological significance of these processes.
组蛋白翻译后修饰通过调节染色质结构和基因转录活性影响许多基本细胞事件。这些修饰高度动态且受到严格控制,有许多酶专门负责这些修饰的添加和去除。有趣的是,这些修饰酶自身在蛋白质周转水平上通过泛素-蛋白酶体加工进行微调并受到精确调控。在此,我们聚焦于以调节组蛋白修饰酶泛素化的机制为中心的最新进展,包括泛素蛋白酶体降解和去泛素化的逆过程。我们还将讨论这些过程潜在的病理生理意义。