Morris Joanna R, Garvin Alexander J
Birmingham Centre for Genome Biology and Institute of Cancer and Genomics, Medical and Dental School, University of Birmingham, Edgbaston, B15 2TT, UK.
Birmingham Centre for Genome Biology and Institute of Cancer and Genomics, Medical and Dental School, University of Birmingham, Edgbaston, B15 2TT, UK.
J Mol Biol. 2017 Nov 10;429(22):3376-3387. doi: 10.1016/j.jmb.2017.05.012. Epub 2017 May 17.
In recent years, our knowledge of the varied role that ubiquitination plays in promoting signal amplification, novel protein interactions, and protein turnover has progressed rapidly. This is particularly remarkable in the examination of how DNA double-stranded breaks (DSBs) are repaired, with many components of the ubiquitin (Ub) conjugation, de-conjugation, and recognition machinery now identified as key factors in DSB repair. In addition, a member of the Ub-like family, small Ub-like modifier (SUMO), has also been recognised as integral for efficient repair. Here, we summarise our emerging understanding of SUMOylation both as a distinct modification and as a cooperative modification with Ub, using the cellular response to DNA DSBs as the primary setting to compare these modifications.
近年来，我们对于泛素化在促进信号放大、新型蛋白质相互作用及蛋白质周转中所起的多种作用的认识迅速发展。这在DNA双链断裂（DSB）修复机制的研究中尤为显著，目前已确定泛素（Ub）缀合、去缀合及识别机制的许多成分是DSB修复的关键因素。此外，类泛素家族成员小泛素样修饰物（SUMO）也被认为是高效修复所必需的。在这里，我们以细胞对DNA DSB的反应作为主要背景来比较这些修饰，总结我们对SUMO化作为一种独特修饰以及与Ub协同修饰的新认识。
