Detection of proteins sumoylated in vivo and in vitro.
Detection of proteins sumoylated in vivo and in vitro.
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DOI：
10.1007/978-1-60327-378-7_17
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发表时间：
2009
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影响因子：
--
通讯作者：
Park-Sarge, Ok-Kyong
中科院分区：
文献类型：
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作者：
Sarge, Kevin D;Park-Sarge, Ok-Kyong
小泛素相关修饰物(SUMO)是一种与多种靶蛋白共价连接的泛素样蛋白。与泛素化不同，苏莫化并不针对蛋白质进行蛋白质分解，而是参与调节多种蛋白质功能特性，包括蛋白质-蛋白质相互作用和亚细胞靶向等。蛋白质和甲基化被认为是许多核过程和核结构的调节者，这使得对这种修饰的表征对于理解核结构和功能至关重要。因此，人们对识别作为这种修饰靶标的新蛋白质并确定它在调节其功能中所起的作用产生了浓厚的兴趣。本章介绍了确定某一特定蛋白质是否为苏莫化底物的方法，以及确定发生修饰的赖氨酸残基(S)的方法。
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 multiple 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 nuclear structure, making the characterization of this modification vital for understanding nuclear structure and function. Consequently, there has been intense interest in identifying new proteins that are targets of this modification and determining what role it plays in regulating their 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.