| First Author | Gao XH | Year | 2015 |
| Journal | Elife | Volume | 4 |
| Pages | e10067 | PubMed ID | 26595448 |
| Mgi Jnum | J:269487 | Mgi Id | MGI:6206904 |
| Doi | 10.7554/eLife.10067 | Citation | Gao XH, et al. (2015) Quantitative H2S-mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response. Elife 4:e10067 |
| abstractText | 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 beta 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 beta cells is coupled to metabolic alternations triggered by sulfhydration of key enzymes in intermediary metabolism. |
