Research ArticlePosttranslational Modifications

H2S Signals Through Protein S-Sulfhydration

Science Signaling  10 Nov 2009:
Vol. 2, Issue 96, pp. ra72
DOI: 10.1126/scisignal.2000464

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Abstract

Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine γ-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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