Issue 5, 2017

Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

Abstract

Protein thiols play a crucial role in redox signaling, in the regulation of enzymatic activity and protein function, and in maintaining redox homeostasis in living systems. The unique chemical reactivity of the thiol group makes protein cysteines susceptible to reactions with reactive oxygen and nitrogen species that form various reversible and irreversible post-translational modifications (PTMs). The reversible PTMs in particular are major components of redox signaling and are involved in the regulation of various cellular processes under physiological and pathological conditions. The biological significance of these redox PTMs in both healthy and disease states has been increasingly recognized. Herein, we review recent advances in quantitative proteomic approaches for investigating redox PTMs in complex biological systems, including general considerations of sample processing, chemical or affinity enrichment strategies, and quantitative approaches. We also highlight a number of redox proteomic approaches that enable effective profiling of redox PTMs for specific biological applications. Although technical limitations remain, redox proteomics is paving the way to a better understanding of redox signaling and regulation in both healthy and disease states.

Graphical abstract: Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

Article information

Article type
Review Article
Submitted
20 Dec 2016
Accepted
21 Mar 2017
First published
27 Mar 2017

Mol. BioSyst., 2017,13, 816-829

Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

J. Duan, M. J. Gaffrey and W. Qian, Mol. BioSyst., 2017, 13, 816 DOI: 10.1039/C6MB00861E

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