Quantitative H2S-mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response.

Fri, 2016-06-24 11:55 -- voskuhlt
TitleQuantitative H2S-mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response.
Publication TypeJournal Article
Year of Publication2015
AuthorsGao X-H, Krokowski D, Guan B-J, Bederman I, Majumder M, Parisien M, Diatchenko L, Kabil O, Willard B, Banerjee R, Wang B, Bebek G, Evans CR, Fox PL, Gerson SL, Hoppel CL, Liu M, Arvan P, Hatzoglou M
JournalElife
Volume4
Paginatione10067
Date Published2015
ISSN2050-084X
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.

DOI10.7554/eLife.10067
Alternate JournalElife
PubMed ID26595448
PubMed Central IDPMC4733038
Grant List1S10RR031537-01 / RR / NCRR NIH HHS / United States
DK48280 / DK / NIDDK NIH HHS / United States
R01 DK048280 / DK / NIDDK NIH HHS / United States
R01 GM112455 / GM / NIGMS NIH HHS / United States
R01-DK013499 / DK / NIDDK NIH HHS / United States
R01-DK053307 / DK / NIDDK NIH HHS / United States
R01-HL58984 / HL / NHLBI NIH HHS / United States
R37-DK060596 / DK / NIDDK NIH HHS / United States
S10 RR031537 / RR / NCRR NIH HHS / United States