Deciphering tissue-specific ubiquitylation by mass spectrometry.
Deciphering tissue-specific ubiquitylation by mass spectrometry.
复制标题
通过质谱法解密组织特异性的泛素化。
DOI：
10.1007/978-1-61779-474-2_3
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Peng, Junmin
中科院分区：
文献类型：
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作者：
Mayor, Ugo;Peng, Junmin
蛋白质泛素化是真核生物中高度保守的调节细胞事件的中心机制，如蛋白酶体降解、蛋白质运输、DNA修复、突触可塑性和免疫应答。蛋白质泛素化的结果由附着在底物上的泛素部分的结构调节，包括泛素单体和具有不同连接的多种聚泛素链（N-末端，K6，K11，K27，K29，K33，K48和K63）。泛素富集策略的发展与灵敏的质谱技术相结合，可以直接分析细胞中的泛素化蛋白，为泛素研究提供了宝贵的工具。在这一章中，我们描述了最近的技术更新，用于分析组织特异性泛素缀合物的转基因模型，以及有针对性的蛋白质组学方法，用于定量不同的多聚泛素链连接在任何类型的样品，包括人体组织。
Protein ubiquitination is a highly conserved, central mechanism to regulate cellular events in all eukaryotes, such as proteasomal degradation, protein trafficking, DNA repair, synaptic plasticity and immune response. The consequence of protein ubiquitination is modulated by the structure of ubiquitin moiety attached on the substrates, including ubiquitin monomer and diverse polyubiquitin chains with different linkages (N-terminus, K6, K11, K27, K29, K33, K48 and K63). The development of ubiquitin-enrichment strategies coupled with sensitive mass spectrometry enables direct analysis of ubiquitinated proteins in cells, providing an invaluable tool for ubiquitin research. In this chapter we describe recent technology updates for analyzing tissue-specific ubiquitin conjugates in transgenic models, as well as targeted proteomics methods for quantifying different polyubiquitin chain linkages in any type of samples, including human tissues.