Proteomic identification of protein ubiquitination events.
Proteomic identification of protein ubiquitination events.
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DOI：
10.1080/02648725.2013.801232
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发表时间：
2013
影响因子：
--
通讯作者：
Jaffrey SR
中科院分区：
文献类型：
--
作者：
Xu G;Jaffrey SR
蛋白质泛素化是一种重要的翻译后修饰（PTM），它调节着真核生物几乎所有方面的细胞功能和许多细胞信号通路。蛋白质泛素化的改变与许多疾病有关，如癌症、神经退行性疾病、心血管疾病、免疫紊乱和炎症性疾病。为了了解蛋白质泛素化在这些疾病和细胞信号通路中的作用，有必要确定泛素化蛋白及其修饰位点。然而，由于蛋白质泛素化的性质，在生理条件下确定确切的修饰位点是具有挑战性的。最近，一种利用单克隆抗体特异性富集来自蛋白质泛素化部分的肽，并利用质谱（MS）进行鉴定的免疫沉淀方法——泛素残体分析（ubiquitin残体profiling）被开发出来，用于测定细胞裂解物中的泛素化事件。这种方法现在已经被广泛应用于在几种细胞环境中分析蛋白质泛素化。本文综述了基于质谱的蛋白质泛素化位点鉴定方法，分析了它们的优缺点，并讨论了它们在泛素化蛋白质组学分析中的应用。
Protein ubiquitination is an important post-translational modification (PTM) that regulates almost every aspect of cellular function and many cell signaling pathways in eukaryotes. Alterations of protein ubiquitination have been linked to many diseases, such as cancer, neurodegenerative diseases, cardiovascular diseases, immunological disorders, and inflammatory diseases. In order to understand the roles of protein ubiquitination in these diseases and in cell signaling pathways, it is necessary to identify ubiquitinated proteins and their modification sites. However, due to the nature of protein ubiquitination, it is challenging to identify the exact modification sites under physiological conditions. Recently, ubiquitin remnant profiling, an immunoprecipitation approach, which utilizes monoclonal antibodies to specifically enrich for peptides derived from the ubiquitinated portion of proteins and mass spectrometry (MS) for their identification, was developed to determine ubiquitination events from cell lysates. This approach has now been widely applied to profile protein ubiquitination in several cellular contexts. In this review, we discuss MS-based methods for the identification of protein ubiquitination sites, analyze their advantages and disadvantages, and discuss their application for proteomic analysis of ubiquitination.
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