Protein S-nitrosylation: A physiological signal for neuronal nitric oxide

Samie R. Jaffrey; Hediye Erdjument-Bromage; Christopher D. Ferris; Paul Tempst; Solomon H. Snyder

doi:10.1038/35055104

Protein S-nitrosylation: A physiological signal for neuronal nitric oxide

Samie R. Jaffrey, Hediye Erdjument-Bromage, Christopher D. Ferris, Paul Tempst, Solomon H. Snyder

School of Medicine

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

1173 Scopus citations

Abstract

Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.

Original language	English (US)
Pages (from-to)	193-197
Number of pages	5
Journal	Nature cell biology
Volume	3
Issue number	2
DOIs	https://doi.org/10.1038/35055104
State	Published - 2001

ASJC Scopus subject areas

Cell Biology

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title = "Protein S-nitrosylation: A physiological signal for neuronal nitric oxide",

abstract = "Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.",

author = "Jaffrey, {Samie R.} and Hediye Erdjument-Bromage and Ferris, {Christopher D.} and Paul Tempst and Snyder, {Solomon H.}",

note = "Funding Information: ACKNOWLEDGEMENTS We thank A. Grewal and A. Nazarian for assistance with mass fingerprinting, A. Kashani for assistance during early stages of this project, and D. Guastella for genotyping the mice. This work was supported by USPHS grants (to S.H.S.), a grant from the National Cancer Institute (to P.T.), a Young Investigator Award from the National Alliance for Research on Schizophrenia and Affective Disorders (to S.R.J.), and a Howard Hughes Fellowship for Physicians (to C.D.F.). Correspondence and requests for materials should be addressed to S.H.S.",

year = "2001",

doi = "10.1038/35055104",

language = "English (US)",

volume = "3",

pages = "193--197",

journal = "Nature cell biology",

issn = "1465-7392",

publisher = "Nature Publishing Group",

number = "2",

}

TY - JOUR

T1 - Protein S-nitrosylation

T2 - A physiological signal for neuronal nitric oxide

AU - Jaffrey, Samie R.

AU - Erdjument-Bromage, Hediye

AU - Ferris, Christopher D.

AU - Tempst, Paul

AU - Snyder, Solomon H.

N1 - Funding Information: ACKNOWLEDGEMENTS We thank A. Grewal and A. Nazarian for assistance with mass fingerprinting, A. Kashani for assistance during early stages of this project, and D. Guastella for genotyping the mice. This work was supported by USPHS grants (to S.H.S.), a grant from the National Cancer Institute (to P.T.), a Young Investigator Award from the National Alliance for Research on Schizophrenia and Affective Disorders (to S.R.J.), and a Howard Hughes Fellowship for Physicians (to C.D.F.). Correspondence and requests for materials should be addressed to S.H.S.

PY - 2001

Y1 - 2001

N2 - Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.

AB - Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.

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JF - Nature cell biology

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Protein S-nitrosylation: A physiological signal for neuronal nitric oxide

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