Park-Sarge Ok-Kyong, Sarge Kevin D
Department of Physiology, University of Kentucky, Lexington, KY, USA.
Methods Mol Biol. 2009;464:255-65. doi: 10.1007/978-1-60327-461-6_14.
Small ubiquitin-related modifier (SUMO) is an ubiquitin-like protein that is covalently attached to a variety of target proteins. Unlike ubiquitination, sumoylation does not target proteins for proteolytic breakdown, but is instead involved in regulating a variety of different protein functional properties, including protein-protein interactions and subcellular targeting, to name a few. Protein sumoylation has been particularly well characterized as a regulator of many nuclear processes as well as of nuclear structure, making the characterization of this modification vital for understanding nuclear structure and function. Because sumoylation plays an important role in regulating so many important cellular processes, there has been intense interest in identifying new proteins that are targets of this modification and determining what role sumoylation plays in regulating the protein functions. This chapter presents methodologies for determining whether a particular protein is a substrate of sumoylation, and for identifying the lysine residue(s) where the modification occurs.
小泛素相关修饰物（SUMO）是一种类泛素蛋白，可共价连接到多种靶蛋白上。与泛素化不同，SUMO化并不将蛋白质靶向蛋白水解降解，而是参与调节多种不同的蛋白质功能特性，包括蛋白质-蛋白质相互作用和亚细胞定位等。蛋白质SUMO化作为许多核过程以及核结构的调节因子已得到特别充分的表征，因此对这种修饰的表征对于理解核结构和功能至关重要。由于SUMO化在调节如此多重要的细胞过程中发挥着重要作用，人们对鉴定作为这种修饰靶标的新蛋白质以及确定SUMO化在调节蛋白质功能中所起的作用产生了浓厚兴趣。本章介绍了确定特定蛋白质是否为SUMO化底物以及鉴定发生修饰的赖氨酸残基的方法。
