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

doi:10.1126/scisignal.2000464

H_S 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

Graduate Studies

Research output: Contribution to journal › Article › peer-review

1145 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 language	English (US)
Pages (from-to)	ra72
Journal	Science Signaling
Volume	2
Issue number	96
DOIs	https://doi.org/10.1126/scisignal.2000464
State	Published - Nov 10 2009

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "HS signals through protein S-Sulfhydration",

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.",

author = "Mustafa, \{Asif K.\} and Gadalla, \{Moataz M.\} and Nilkantha Sen and Seyun Kim and Weitong Mu and Gazi, \{Sadia K.\} and Barrow, \{Roxanne K.\} and Guangdong Yang and Rui Wang and Snyder, \{Solomon H.\}",

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T1 - HS signals through protein S-Sulfhydration

AU - Mustafa, Asif K.

AU - Gadalla, Moataz M.

AU - Sen, Nilkantha

AU - Kim, Seyun

AU - Mu, Weitong

AU - Gazi, Sadia K.

AU - Barrow, Roxanne K.

AU - Yang, Guangdong

AU - Wang, Rui

AU - Snyder, Solomon H.

PY - 2009/11/10

Y1 - 2009/11/10

N2 - 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.

AB - 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.

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VL - 2

SP - ra72

JO - Science Signaling

JF - Science Signaling

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ER -

H_S signals through protein S-Sulfhydration

Abstract

ASJC Scopus subject areas

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