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Updated: Mar 29, 2026

Measurements of Physiological Stress Responses in C. Elegans
Published on: May 21, 2020
Quantitative H2S-mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response
Xing-Huang Gao1, Dawid Krokowski1, Bo-Jhih Guan1
1Department of Genetics and Genome Sciences, Case Western Reserve University, Cleveland, United States.
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.
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