H 2 S Signals Through Protein S-Sulfhydration
Johns Hopkins University · Johns Hopkins Medicine · +1 more institution
Abstract
Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine gamma-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. We now show that H2S physiologically modifies cysteines in a large number of proteins by S-sulfhydration. About 10 to 25% of many liver proteins, including actin, tubulin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are sulfhydrated under physiological conditions. Sulfhydration augments GAPDH activity and enhances actin polymerization. Sulfhydration thus appears to be a physiologic posttranslational modification for proteins.
Citation impact
- FWCI
- 27.05
- Percentile
- 100%
- References
- 21
Authors
10- AKAsif K. Mustafa
Johns Hopkins University, Johns Hopkins Medicine
- MMMoataz M. Gadalla
Johns Hopkins University, Johns Hopkins Medicine
- NSNilkantha Sen
Johns Hopkins University, Johns Hopkins Medicine
- SKSeyun Kim
Johns Hopkins University, Johns Hopkins Medicine
- WMWeitong Mu
Johns Hopkins University, Johns Hopkins Medicine
Topics & keywords
- Hydrogen sulfide
- Cysteine
- Chemistry
- Biochemistry
- Hydrogen sulphide
- Enzyme
- Sulfur
- Organic chemistry