Research ArticlePosttranslational Modifications

H2S Signals Through Protein S-Sulfhydration

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

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Battling for the Same Cysteine?

Recent evidence suggests that hydrogen sulfide (H2S)—a gas perhaps best known for its scent of rotten eggs—has joined nitric oxide (NO) and carbon monoxide in the select ranks of gases that act as physiologic messenger molecules. Although H2S is enzymatically generated in vivo and mediates various physiologic functions, including acting as a vasorelaxant and eliciting hibernation states, the mechanisms through which it affects its targets have been unclear. Here, Mustafa et al. show that endogenous H2S modifies cysteine residues in many proteins, including glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and actin, converting cysteine -SH groups to -SSH groups in a process the authors call S-sulfhydration. Intriguingly, H2S enhanced GAPDH activity through sulfhydration of a cysteine residue that is also a target of nitrosylation by NO, which inhibits GAPDH activity, suggesting that some targets might be subject to regulation through competitive nitrosylation and sulfhydration of the same cysteine residues.