泛素及其类似物的蛋白质组学研究进展

Proteomic approaches to post-translational modification by ubiquitin family proteins

作为蛋白质的翻译后修饰,泛素及其类似物(ubiquitin-like modifiers,Ubls)对底物的修饰被认为是真核细胞内一种重要的调节机制。根据以往的研究表明,泛素/ubls与各种各样的底物蛋白形成共价结合以后,通过介导蛋白质降解、改变蛋白质的细胞定位、改变蛋白质的酶活性、改变蛋白质之间的相互作用等影响这些底物的功能与活性。可以想象,通过影响成百上千的不同底物蛋白,泛素和Ubls在各个细胞生理活动中都发挥着重要的调节作用。运用蛋白质组学的方法对泛素/Ubls进行研究,可以发现更多新的泛素和ubls的底物,帮助人们从整体水平上了解泛素/Ubls这个复杂的修饰系统。而利用质谱技术精确的鉴定泛素/Ubls在底物上的修饰位点则为进一步研究修饰发生的分子机制,以及对底物蛋白功能的影响提供了明确的线索和方向。到目前为止,已有越来越多的科学家们对泛素/Ubls修饰的蛋白质组学感兴趣并致力于这方面的研究,取得了很大进展。本文对泛素及Ubls的蛋白质组学研究进展进行了归纳和总结。

Post-translational modification by ubiquitin and ubiquitin-like modifiers（Ubls） is one of the most important mechanisms regulating a wide range of cellular processes in eukaryotes. Previous research showed that, through covalently modification by ubiquitin or ubls, the substrate proteins can be regulated in many different ways like stability, subcellular localization, enzymatic activity, protein-protein interaction and so on. Therefore, we believe, that ubiquitin and ubls play very important roles in cellular and biological processes by modifying plenty of proteins. To better understand the ubiquitin and ubls system, proteomic approaches have been developed to purify and identify more protein substrates. Large-scale idendification of ubiquitin/ubls - modification sites by mass spectrometry is particularly important for understanding the molecular mechanism and function of ubiquitin/ubls modification. Upto the present, more and more scientists are getting interested and participating in proteomics research of ubiquitin/ Ubl modifications. This review summarizes the rencent results in this field.