HS signals through protein S-Sulfhydration

Asif K. Mustafa, Moataz M. Gadalla, Nilkantha Sen, Seyun Kim, Weitong Mu, Sadia K. Gazi, Roxanne K. Barrow, Guangdong Yang, Rui Wang, Solomon H. Snyder

Research output: Contribution to journalArticle

698 Scopus citations

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 languageEnglish (US)
Pages (from-to)ra72
JournalScience Signaling
Volume2
Issue number96
DOIs
StatePublished - Nov 10 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Mustafa, A. K., Gadalla, M. M., Sen, N., Kim, S., Mu, W., Gazi, S. K., Barrow, R. K., Yang, G., Wang, R., & Snyder, S. H. (2009). HS signals through protein S-Sulfhydration. Science Signaling, 2(96), ra72. https://doi.org/10.1126/scisignal.2000464