Glutathione S-Transferase P-Mediated Protein S-Glutathionylation of Resident Endoplasmic Reticulum Proteins Influences Sensitivity to Drug-Induced Unfolded Protein Response

• Published in: Antioxidants & redox signaling Vol. 26; no. 6; p. 247
• Main Authors: Ye, Zhi-Wei, Zhang, Jie, Ancrum, Tiffany, Manevich, Yefim, Townsend, Danyelle M, Tew, Kenneth D
• Format: Journal Article
• Language: English
• Published: United States 20.02.2017
• Subjects: Animals; Calcium - metabolism; Cell Line; Drug Discovery; Endoplasmic Reticulum - metabolism; Endoplasmic Reticulum Stress - drug effects; Gene Expression Regulation - drug effects; Glutathione - metabolism; Glutathione Transferase - genetics; Glutathione Transferase - metabolism; Liver - drug effects; Liver - metabolism; Mice; Mice, Knockout; Models, Biological; Protein Binding; Protein Interaction Mapping; Protein Processing, Post-Translational - drug effects; Protein S - metabolism; Protein Transport; Reactive Oxygen Species - metabolism; Unfolded Protein Response - drug effects; Unfolded Protein Response - genetics; unfolded protein response; dendritic cells; protein disulfide isomerase; S-glutathionylation; endoplasmic reticulum; glutathione S-transferases

S-glutathionylation of cysteine residues, catalyzed by glutathione S-transferase Pi (GSTP), alters structure/function characteristics of certain targeted proteins. Our goal is to characterize how S-glutathionylation of proteins within the endoplasmic reticulum (ER) impact cell sensitivity to ER-stre...