H <sub>2</sub> S Signals Through Protein S-Sulfhydration
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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.
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The record
- Venue
- Science Signaling
- Topic
- Sulfur Compounds in Biology
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- Lakehead University
- Funders
- National Institute of General Medical SciencesNational Institute on Drug AbuseNational Institute of Mental HealthCanadian Institutes of Health Research
- Keywords
- Hydrogen sulfideCysteineChemistryBiochemistryHydrogen sulphideEnzymeSulfurOrganic chemistry
- Has abstract in OpenAlex
- yes