Wilson Van G, Heaton Phillip R
Department of Microbial & Molecular Pathogenesis, College of Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114, USA.
Expert Rev Proteomics. 2008 Feb;5(1):121-35. doi: 10.1586/14789450.5.1.121.
The small ubiquitin-like modifier proteins (Smt3 in yeast and SUMOs 1-4 in vertebrates) are members of the ubiquitin super family. Like ubiquitin, the SUMOs are protein modifiers that are covalently attached to the epsilon-amino group of lysine residues in the substrates. The application of proteomics to the SUMO field has greatly expanded both the number of known targets and the number of identified target lysines. As new refinements of proteomic techniques are developed and applied to sumoylation, an explosion of novel data is likely in the next 5 years. This ability to examine sumoylated proteins globally, rather than individually, will lead to new insights into both the functions of the individual SUMO types, and how dynamic changes in overall sumoylation occur in response to alterations in cellular environment. In addition, there is a growing appreciation for the existence of cross-talk mechanisms between the sumoylation and ubiquitinylation processes. Rather than being strictly parallel, these two systems have many points of intersection, and it is likely that the coordination of these two systems is a critical contributor to the regulation of many fundamental cellular events.
小泛素样修饰蛋白(酵母中的Smt3和脊椎动物中的SUMO 1 - 4)是泛素超家族的成员。与泛素一样,SUMO是蛋白质修饰剂,可共价连接到底物中赖氨酸残基的ε-氨基上。蛋白质组学在SUMO领域的应用极大地增加了已知靶标的数量和已鉴定的靶标赖氨酸的数量。随着蛋白质组学技术的新改进被开发并应用于SUMO化,未来5年可能会出现大量新数据。这种全局而非单独检测SUMO化蛋白质的能力,将为单个SUMO类型的功能以及整体SUMO化如何响应细胞环境变化而发生动态变化带来新的见解。此外,人们越来越认识到SUMO化和泛素化过程之间存在相互作用机制。这两个系统并非严格平行,而是有许多交叉点,并且这两个系统的协调很可能是许多基本细胞事件调控的关键因素。