The Redox Code involves specific, reversible oxidative changes in proteins that modulate protein tertiary structure, interactions, trafficking, and activity, and hence couple the proteome to the metabolic/oxidative state of cells. It is currently a major focus of study in cell biology. Recent studies of dynamic cellular spatial reorganization with MS‐based subcellular‐spatial‐razor proteomics reveal that protein constituents of many subcellular structures, including mitochondria, the endoplasmic reticulum, the plasma membrane, and the extracellular matrix, undergo changes in their subcellular abundance/distribution in response to oxidative stress. These proteins are components of a diverse variety of functional processes spatially distributed across cells. Many of the same proteins are involved in response to suppression of DNA replication indicate that oxidative stress is strongly intertwined with DNA replication/proliferation. Both are replete with networks of moonlighting proteins that show coordinated changes in subcellular location and that include primary protein actuators of the redox code involved in the processing of NAD⁺/NADH, NADP⁺/NADPH, Cys/CySS, and GSH/GSSG redox couples. Small groups of key proteins such as {KPNA2, KPNB1, PCNA, PTMA, SET} constitute “spatial switches” that modulate many nuclear processes. Much of the functional response involves subcellular protein trafficking, including nuclear import/export processes, vesicle‐mediated trafficking, the endoplasmic reticulum/Golgi pathway, chaperone‐assisted processes, and other transport systems. This is not visible to measurements of total protein abundance by transcriptomics or proteomics. Comprehensive pictures of cellular function will require collection of data on the subcellular transport and local functions of many moonlighting proteins, especially of those with critical roles in spatial coordination across cells. The proteome‐wide analysis of coordinated changes in abundance and trafficking of proteins offered by MS‐based proteomics has a unique, crucial role to play in deciphering the complex adaptive systems that underlie cellular function. © 2016 Wiley Periodicals, Inc. Mass Spec Rev

中文翻译：

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氧化还原代码中的空间观点—月光照蛋白质的质谱光谱蛋白质组学研究

氧化还原法涉及蛋白质中特定的，可逆的氧化变化，可调节蛋白质的三级结构，相互作用，运输和活性，从而将蛋白质组与细胞的代谢/氧化状态结合。目前，它是细胞生物学研究的主要重点。基于基于MS的亚细胞空间剃刀蛋白质组学的动态细胞空间重组的最新研究表明，许多亚细胞结构的蛋白质成分（包括线粒体，内质网，质膜和细胞外基质）的亚细胞丰度/分布发生变化。应对氧化应激。这些蛋白质是空间分布在整个细胞中的各种功能过程的组成部分。许多相同的蛋白质都参与了对DNA复制抑制的反应，这表明氧化应激与DNA复制/增殖密切相关。两者都充满了月光照下的蛋白质网络，这些网络显示出亚细胞位置的协调变化，并且包括参与NAD加工的氧化还原代码的主要蛋白质促动器⁺ / NADH，NADP ⁺/ NADPH，Cys / CySS和GSH / GSSG氧化还原对。一小群关键蛋白质，例如{KPNA2，KPNB1，PCNA，PTMA，SET}构成了调节许多核过程的“空间开关”。许多功能反应涉及亚细胞蛋白运输，包括核进出口过程，囊泡介导的运输，内质网/高尔基体通路，伴侣辅助过程和其他运输系统。这对于通过转录组学或蛋白质组学测量总蛋白丰度是不可见的。要全面了解细胞功能，就需要收集有关许多月光照蛋白，尤其是在跨细胞空间协调中起关键作用的蛋白的亚细胞转运和局部功能的数据。基于蛋白质组的蛋白质组学所提供的蛋白质丰度和运输的协调变化的蛋白质组范围分析在破译细胞功能基础的复杂适应性系统中具有独特而至关重要的作用。©2016 Wiley Periodicals，Inc.质谱修订版