| First Author | McGarry DJ | Year | 2015 |
| Journal | Biochem J | Volume | 469 |
| Issue | 1 | Pages | 25-32 |
| PubMed ID | 25891661 | Mgi Jnum | J:225856 |
| Mgi Id | MGI:5694569 | Doi | 10.1042/BJ20141256 |
| Citation | McGarry DJ, et al. (2015) Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver. Biochem J 469(1):25-32 |
| abstractText | 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. |
