Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture

Forrester, Michael T.; Thompson, J. Will; Foster, Matthew W.; Nogueira, Leonardo; Moseley, M. Arthur; Stamler, Jonathan S.

doi:10.1038/nbt.1545

Cited by 341 publications

(391 citation statements)

References 15 publications

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“…Nitrosylation of Prx1 in Cells-To investigate S-nitrosylation of endogenous Prx1, we exposed RAW264.7 macrophages to CysNO treatment and assayed for SNO-Prx1 formation with the SNO-RAC method (21). Similar to the in vitro results, endogenous Prx1 was rapidly nitrosylated in response to treatment with CysNO, with maximal nitrosylation observed at the 5-min time point (Fig.…”

Section: Table 1 the Characteristics Of Reduced And Nitrosylated Prx1supporting

confidence: 53%

“…Nitrosylation likewise inhibits the activity of plant Prx II E (20). Prx1 was found to be nitrosylated in endotoxin-stimulated macrophages (21,22), and recent studies indicate that nitrosylation protects Prx1 from over-oxidation (23). Despite these reports, it remains to be established exactly how S-nitrosylation controls the structure and function of distinct Prx proteins and, more generally, how and to what extent SNOs and H 2 O 2 cross-regulate each other's function.…”

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confidence: 95%

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Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

Engelman

Weisman-Shomer

Ziv

et al. 2013

Journal of Biological Chemistry

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Background: S-Nitrosylation may regulate 2-Cys peroxiredoxin systems to affect cellular metabolism of hydrogen peroxide. Results: Nitrosylation impeded the peroxiredoxin-1 catalytic cycle by directly inhibiting the activity of peroxiredoxin-1 and by interfering with the recycling of oxidized peroxiredoxin-1 by the thioredoxin system. Conclusion: Nitrosylation exerts multilevel control of the thioredoxin-peroxiredoxin system. Significance: Through its multiple effects on the thioredoxin-peroxiredoxin system, nitrosylation may influence cellular redox homeostasis.

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Section: Table 1 the Characteristics Of Reduced And Nitrosylated Prx1supporting

confidence: 53%

mentioning

confidence: 95%

Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

Engelman

Weisman-Shomer

Ziv

et al. 2013

Journal of Biological Chemistry

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“…Accordingly, in most instances, the time course of these processes might not be rate limiting for the overall events that comprise NMDAR activation, stimulation of nNOS to generate NO, nitrosylation of stargazin, and its translocation along with GluR1. However, in some cases, both basal and stimulated denitrosylation take place over varied time scales (20)(21)(22)(23)(24). In the case of stargazin-mediated GluR1 surface expression, nitrosylation of stargazin does not have an obligate role in trafficking; instead, it exerts a regulatory influence.…”

Section: Discussionmentioning

confidence: 99%

S-nitrosylation of stargazin regulates surface expression of AMPA-glutamate neurotransmitter receptors

Selvakumar

Huganir

Snyder

2009

Proc. Natl. Acad. Sci. U.S.A.

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Synaptic plasticity is mediated by changes in the surface expression of AMPA receptors (AMPARs). Stargazin and related transmembrane AMPAR regulatory proteins have emerged as the principal regulators of AMPAR surface expression. Here, we show in heterologous cells and primary neurons that stargazin is physiologically S-nitrosylated, resulting in increased surface expression. Snitrosylation of stargazin increases binding to the AMPAR subunit GluR1, causing increased surface expression of the AMPAR. NMDAR stimulation, well known to activate neuronal nitric oxide synthase, increases both nitrosylation of stargazin and its binding to AMPAR. Thus, S-nitrosylation of stargazin is a physiologic regulator of AMPAR surface expression.

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“…2C) have been previously identified by MS-based analyses of SNO-treated RAW246.7 macrophages or brain extracts, respectively (23,50,61). Inasmuch as the in vitro targets of SNOs (e.g., in tissue extracts) have been shown to significantly overlap the sets of proteins that are S-nitrosylated by endogenous NO (21), protein microarrays present a tractable methodology for deconvoluting the multiple pathways for S-nitrosylation and denitrosylation that govern steady-state SNO levels in vivo (12,61,62).…”

Section: Discussionmentioning

confidence: 99%

A protein microarray-based analysis of S -nitrosylation

Foster

Forrester

Stamler

2009

Proc. Natl. Acad. Sci. U.S.A.

105

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The ubiquitous cellular influence of nitric oxide (NO) is exerted substantially through protein S-nitrosylation. Whereas NO is highly promiscuous, physiological S-nitrosylation is typically restricted to one or very few Cys residue(s) in target proteins. The molecular basis for this specificity may derive from properties of the target protein, the S-nitrosylating species, or both. Here, we describe a protein microarray-based approach to investigate determinants of S-nitrosylation by biologically relevant low-mass S-nitrosothiols (SNOs). We identify large sets of yeast and human target proteins, among which those with active-site Cys thiols residing at N termini of ␣-helices or within catalytic loops were particularly prominent. However, S-nitrosylation varied substantially even within these families of proteins (e.g., papain-related Cys-dependent hydrolases and rhodanese/Cdc25 phosphatases), suggesting that neither secondary structure nor intrinsic nucleophilicity of Cys thiols was sufficient to explain specificity. Further analyses revealed a substantial influence of NO-donor stereochemistry and structure on efficiency of S-nitrosylation as well as an unanticipated and important role for allosteric effectors. Thus, high-throughput screening and unbiased proteome coverage reveal multifactorial determinants of S-nitrosylation (which may be overlooked in alternative proteomic analyses), and support the idea that target specificity can be achieved through rational design of S-nitrosothiols.cysteine ͉ nitric oxide ͉ S-nitrosothiol ͉ thiol P rotein S-nitrosylation underlies much of the physiological signaling by both nitric oxide (NO) and endogenous Snitrosothiols, and both hypo-and hyper-S-nitrosylation have been causally implicated in disease (1, 2). Formally, Snitrosylation occurs either via an oxidative reaction of NO and Cys thiol, in the presence of an electron acceptor (e.g., transition metal or O 2 ), or by the transfer of NO ϩ (transnitros(yl)ation) from donor S-nitrosothiol (SNO) to acceptor Cys thiol (1). These reactions may be enzyme-catalyzed or otherwise facilitated. For example, hemoglobin and ceruloplasmin support metaldependent S-nitrosylation (3-5) whereas S-nitroso-hemoglobin (SNO-hemoglobin) and SNO-thioredoxin can transnitrosylate proteins with which they interact directly (anion exchanger 1 and caspase-3, respectively) (6, 7). Transnitrosylation is also implicated in protein S-nitrosylation coupled to NO synthase activity (8-10) and involves the intermediacy of the endogenous lowmass SNO, S-nitrosoglutathione (GSNO), as evidenced by elevated levels of SNO-proteins in mice lacking the GSNO metabolizing enzyme, GSNO reductase (GSNOR) (8-11). GSNOR deletion also increases S(NO)-mediated protein S-nitrosylation and cytostasis in yeast (11,12), and decreases virulence of several pathogens (13, 14), which suggests that transnitrosylation is an important mediator of nitrosative stress. In addition, metabolism of GSNO to S-nitrosocyteinylglycine and S-nitrosocysteine (CysNO) and CysNO uptake via l-amino...

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Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture

Cited by 341 publications

References 15 publications

Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

S-nitrosylation of stargazin regulates surface expression of AMPA-glutamate neurotransmitter receptors

A protein microarray-based analysis of S -nitrosylation

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