Unknown

Dataset Information

0

H2S signals through protein S-sulfhydration.


ABSTRACT: 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.

SUBMITTER: Mustafa AK 

PROVIDER: S-EPMC2998899 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications


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 act  ...[more]

Similar Datasets

| S-EPMC4733038 | biostudies-literature
| S-EPMC7069468 | biostudies-literature
| S-EPMC7069459 | biostudies-literature
| S-EPMC3328411 | biostudies-literature
| S-EPMC6029264 | biostudies-literature
| S-EPMC3745995 | biostudies-literature
| S-EPMC4306352 | biostudies-literature
| S-EPMC3837443 | biostudies-literature
| S-EPMC7086210 | biostudies-literature
| S-EPMC6152389 | biostudies-literature