H2S signals through protein S-sulfhydration.
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.
Mustafa
Asif K
AK
Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Gadalla
Moataz M
MM
Sen
Nilkantha
N
Kim
Seyun
S
Mu
Weitong
W
Gazi
Sadia K
SK
Barrow
Roxanne K
RK
Yang
Guangdong
G
Wang
Rui
R
Snyder
Solomon H
SH
D000199:Actins / Q000378:metabolism; D000818:Animals; D001704:Biopolymers / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D006862:Hydrogen Sulfide / Q000378:metabolism*; D051379:Mice; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D053719:Tandem Mass Spectrometry; D014404:Tubulin / Q000378:metabolism
D000199:Actins; D001704:Biopolymers; D013438:Sulfhydryl Compounds; D014404:Tubulin; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D006862:Hydrogen Sulfide