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- Title
Quantitative H<sub>2</sub>S-mediated protein sulfhydration reveals metabolic reprogramming during the Integrated Stress Response.
- Authors
Xing-Huang Gao; Krokowski, Dawid; Bo-Jhih Guan; Hatzoglou, Maria; Gerson, Stanton L.; Bederman, Ilya; Majumder, Mithu; Hoppel, Charles L.; Parisien, Marc; Diatchenko, Luda; Kabil, Omer; Banerjee, Ruma; Willard, Belinda; Wang, Benlian; Bebek, Gurkan; Evans, Charles R.; Ming Liu; Arvan, Peter; Fox, Paul L.
- Abstract
The sulfhydration of cysteine residues in proteins is an important mechanism involved in diverse biological processes. We have developed a proteomics approach to quantitatively profile the changes of sulfhydrated cysteines in biological systems. Bioinformatics analysis revealed that sulfhydrated cysteines are part of a wide range of biological functions. In pancreatic β cells exposed to endoplasmic reticulum (ER) stress, elevated H2S promotes the sulfhydration of enzymes in energy metabolism and stimulates glycolytic flux. We propose that transcriptional and translational reprogramming by the Integrated Stress Response (ISR) in pancreatic β cells is coupled to metabolic alternations triggered by sulfhydration of key enzymes in intermediary metabolism.
- Subjects
CYSTEINE; ENDOPLASMIC reticulum; PANCREATIC acinar cells
- Publication
eLife, 2015, p1
- ISSN
2050-084X
- Publication type
Article
- DOI
10.7554/eLife.10067