Quantitative H2S-mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 26595448.
- Also identified by DOI 10.7554/eLife.10067 and PMC identifier 4733038.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Cysteine
- Gene Expression Regulation
- Hydrogen Sulfide
- Metabolic Networks and Pathways
- Protein Processing, Post-Translational
- Stress, Physiological