Abstract
Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine g-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. Wenow show that H2S physiologically modifies cysteines in a large number of proteins byS-sulfhydration.About 10 to 25% ofmany liver proteins, includingactin, tubulin, andglyceraldehyde-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.
Original language | English (US) |
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Pages (from-to) | ra72 |
Journal | Science Signaling |
Volume | 2 |
Issue number | 96 |
DOIs | |
State | Published - Nov 10 2009 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology