Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for GST Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model.
Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver
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David J. McGarry, Wenzhang Chen, Probir Chakravarty, Douglas L. Lamont, C. Roland Wolf, Colin J. Henderson; Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver. Biochem J 1 July 2015; 469 (1): 25–32. doi: https://doi.org/10.1042/BJ20141256
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