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Revealing the functional roles of tyrosine sulfation using synthetic sulfopeptides and sulfoproteins.
Current Opinion in Chemical Biology ( IF 7.8 ) Pub Date : 2020-08-07 , DOI: 10.1016/j.cbpa.2020.05.007
Joshua W C Maxwell 1 , Richard J Payne 1
Affiliation  

The decoration of proteins with post-translational modifications (PTMs) serves as a mechanism to expand the functional repertoire of the proteome. Tyrosine sulfation is a PTM that has been shown to be a key regulator of extracellular protein-protein interactions in a select number of examples. However, the challenges associated with identifying and characterising the functional consequences of tyrosine sulfation have hindered our ability to understand the full scope of its role in the wider proteome when compared with that of other PTMs, for example, phosphorylation and glycosylation. In this account, we highlight recent advances in the prediction and detection of tyrosine sulfation and outline the need for continued innovation in this area. We also discuss the utility of emerging solid-phase synthesis and peptide ligation strategies for accessing libraries of homogeneously sulfated peptides and proteins to help reveal functional aspects of the sulfoproteome.

中文翻译:

使用合成硫肽和硫蛋白揭示酪氨酸硫酸化的功能作用。

具有翻译后修饰 (PTM) 的蛋白质修饰是一种扩展蛋白质组功能库的机制。酪氨酸硫酸化是一种 PTM,在一些选定的例子中已被证明是细胞外蛋白质-蛋白质相互作用的关键调节剂。然而,与其他 PTM(例如磷酸化和糖基化)相比,与识别和表征酪氨酸硫酸化的功能后果相关的挑战阻碍了我们了解其在更广泛蛋白质组中的全部作用的能力。在这篇文章中,我们重点介绍了酪氨酸硫酸化预测和检测方面的最新进展,并概述了该领域持续创新的必要性。
更新日期:2020-08-07
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