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Incidence and physiological relevance of protein thiol switches

机译：蛋白质硫醇开关的发生率和生理相关性

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摘要

A few small-molecule oxidants, most notably hydrogen peroxide, can act as messengers in signal transduction. They trigger so-called 'thiol switches', cysteine residues that are reversibly oxidized to transiently change the functional properties of their host proteins. The proteome-wide identification of functionally relevant 'thiol switches' is of significant interest. Unfortunately, prediction of redox-active cysteine residues on the basis of surface accessibility and other computational parameters appears to be of limited use. Proteomic thiol labeling approaches remain the most reliable strategy to discover new thiol switches in a hypothesis-free manner. We discuss if and how genomic knock-in strategies can help establish the physiological relevance of a 'thiol switch' on the organismal level. We conclude that surprisingly few attempts have been made to thoroughly verify the physiological relevance of thiol-based redox switches in mammalian model organisms.
机译：几种小分子氧化剂，尤其是过氧化氢，可以充当信号转导的信使。它们触发所谓的“硫醇开关”，半胱氨酸残基被可逆氧化，以瞬时改变其宿主蛋白的功能特性。蛋白质组范围内功能相关的“硫醇开关”的识别具有重大意义。不幸的是，基于表面可及性和其他计算参数预测氧化还原活性的半胱氨酸残基似乎用途有限。蛋白质组学巯基标记方法仍然是最可靠的策略，以无假设的方式发现新的巯基开关。我们讨论基因组敲入策略是否以及如何帮助建立生物水平上“硫醇开关”的生理相关性。我们得出的结论是，出乎意料的是，很少进行尝试来全面验证哺乳动物模型生物中基于硫醇的氧化还原开关的生理相关性。

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