Quantitative proteomics to decipher ubiquitin signaling.

Quantitative proteomics to decipher ubiquitin signaling.
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定量蛋白质组学以破译泛素信号传导。

DOI:
10.1007/s00726-012-1286-y
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发表时间:
2012-09
期刊:
影响因子:
3.5
通讯作者:
Peng J
Peng J
中科院分区:
生物学3区
文献类型:
--
作者:
Chen PC;Na CH;Peng J

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在真核生物中,泛素信号转导在控制细胞过程中起着至关重要的作用,并且泛素调节的受损有助于多种人类疾病的发病机制。在过去的十年中,基于质谱的蛋白质组学已经成为鉴定泛素化蛋白、泛素修饰位点、复杂泛素链的结构以及泛素酶的相互作用组的不可或缺的方法。特别是,定量策略的实施可以检测遍在蛋白质组的动态变化,增强区分功能相关蛋白质靶点和生物学和实验变异引起的假阳性的能力。总细胞裂解物和泛素化蛋白质组在同一组样品中的分析已经成为一个强大的工具,揭示了特定的生理和病理条件下,如基因突变的泛素信号调节的底物的子集。这一策略同样适用于分析泛素样蛋白的通路。
Ubiquitin signaling plays an essential role in controlling cellular processes in eukaryotes, and the impairment of ubiquitin regulation contributes to the pathogenesis of a wide range of human diseases. During the last decade, mass spectrometry–based proteomics has emerged as an indispensable approach for identifying ubiquitinated proteins, ubiquitin modification sites, the structure of complex ubiquitin chains, as well as the interactome of ubiquitin enzymes. In particular, implementation of quantitative strategies allows the detection of dynamic changes in the ubiquitinated proteome, enhancing the ability to differentiate between function-relevant protein targets and false positives arising from biological and experimental variations. The profiling of total cell lysate and ubiquitinated proteome in the same sets of samples has become a powerful tool, revealing a subset of substrates that are modulated by specific physiological and pathological conditions, such as gene mutations in ubiquitin signaling. This strategy is equally useful for dissecting the pathways of ubiquitin-like proteins.
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