Mechanisms of Nitrosylation and Denitrosylation of Cytoplasmic Glyceraldehyde-3-phosphate Dehydrogenase from Arabidopsis thaliana

Zaffagnini, Mirko; Morisse, Samuel; Bedhomme, Mariette; Marchand, Christophe; Festa, Margherita; Rouhier, Nicolas; Lemaire, Stéphane D.; Trost, Paolo

doi:10.1074/jbc.m113.475467

Cited by 106 publications

(95 citation statements)

References 94 publications

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“…In addition, there are various indications that S-nitrosylation of GAPDH can lead either to adaptation and acclimation of metabolism under stress conditions, or to cell death in order to prevent any further metabolism and ROS/RNS generation (Romero-Puertas et al, 2013). Arabidopsis GapC1 and 2 are modified and thereby reversibly inactivated, and S-nitrosylation as well as S-glutathionylation could be seen in vitro to occur at both cysteine residues (Holtgrefe et al, 2008;Zaffagnini et al, 2013). Velocity and extent of the modifications likely depend on the presence of metabolites similar to light-dark modulation of chloroplast enzymes.…”

Section: Role Of Gapdh In Acclimation and Cell Protectionmentioning

confidence: 99%

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

Hildebrandt¹,

Knuesting²,

Berndt³

et al. 2015

Biological Chemistry

158

131

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Cytosolic glyceraldehyde 3-phosphate dehydrogenase (GAPDH, E.C. 1.2.1.12) is present in all organisms and catalyzes the oxidation of triose phosphate during glycolysis. GAPDH is one of the most prominent cellular targets of oxidative modifications when reactive oxygen and nitrogen species are formed during metabolism and under stress conditions. GAPDH harbors a strictly conserved catalytic cysteine, which is susceptible to a variety of thiol modifications, including S-sulfenylation, S-glutathionylation, S-nitrosylation, and S-sulfhydration. Upon reversible oxidative thiol modification of GAPDH, glycolysis is inhibited leading to a diversion of metabolic flux through the pentose-phosphate cycle to increase NADPH production. Furthermore, oxidized GAPDH may adopt new functions in different cellular compartments including the nucleus, as well as in new microcompartments associated with the cytoskeleton, mitochondria and plasma membrane. This review focuses on the recently discovered mechanism underlying the eminent reactivity between GAPDH and hydrogen peroxide and the subsequent redox-dependent moonlighting functions discriminating between the induction either of adaptive responses and adjustment of metabolism or of cell death in yeast, plants, and mammals. In light of the summarized results, cytosolic GAPDH might function as a sensor for redox signals and an information hub to transduce these signals for appropriate responses.

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Section: Role Of Gapdh In Acclimation and Cell Protectionmentioning

confidence: 99%

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

Hildebrandt¹,

Knuesting²,

Berndt³

et al. 2015

Biological Chemistry

158

131

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“…Although S-nitrosylation typically inhibits protein function (Hess and Stamler, 2012;Zaffagnini et al, 2013), the effect of S-sulfhydration can either activate, as has been described for glyceraldehyde-3-phosphate dehydrogenase and Parkin E3 ligase activity (Mustafa et al, 2009a;Vandiver et al, 2013), or inactivate enzymatic activities, as has been reported for PTP1B (Krishnan et al, 2011). In other cases, S-sulfhydration has been shown to modify protein-protein interactions, such as in the case of Kelch-like ECH-associated protein1 (Keap1), which acts as a negative regulator of Nuclear factor (erythroid-derived2)-like2 (Nrf2), a master regulator of the antioxidant response in mice (Yang et al, 2013).…”

mentioning

confidence: 99%

S-Sulfhydration: A Cysteine Posttranslational Modification in Plant Systems

et al. 2015

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Hydrogen sulfide is a highly reactive molecule that is currently accepted as a signaling compound. This molecule is as important as carbon monoxide in mammals and hydrogen peroxide in plants, as well as nitric oxide in both eukaryotic systems. Although many studies have been conducted on the physiological effects of hydrogen sulfide, the underlying mechanisms are poorly understood. One of the proposed mechanisms involves the posttranslational modification of protein cysteine residues, a process called S-sulfhydration. In this work, a modified biotin switch method was used for the detection of Arabidopsis (Arabidopsis thaliana) proteins modified by S-sulfhydration under physiological conditions. The presence of an S-sulfhydration-modified cysteine residue on cytosolic ascorbate peroxidase was demonstrated using liquid chromatography-tandem mass spectrometry analysis, and a total of 106 S-sulfhydrated proteins were identified. Immunoblot and enzyme activity analyses of some of these proteins showed that the sulfide added through S-sulfhydration reversibly regulates the functions of plant proteins in a manner similar to that described in mammalian systems.

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“…6, GAPC1) was reduced to undetectable levels only following GSH treatment (lane 4) but not when the TRX system was used (lane 5). The specific denitrosylation of GAPC1 by glutathione has been demonstrated before (Zaffagnini et al, 2013b) and confirms reliability of the in vitro assay. As additional specificity controls for the assay, the absence of biotin label on NAB1 or GAPC1 cysteines was demonstrated after omitting ascorbate (Fig.…”

Section: Nab1 Can Be Efficiently Denitrosylated By Thioredoxin H1 In mentioning

confidence: 66%

“…2A; GSH+H 2 O 2 ). The recombinant Arabidopsis (Arabidopsis thaliana) cytosolic glyceraldehyde-3-phosphate dehydrogenase GAPC1 was used as control since this enzyme is a well established model protein undergoing both glutathionylation and nitrosylation (Zaffagnini et al, 2013b). Mass spectrometry showed that GAPC1 is shifted by 305 D after glutathionylation treatment, while this is not the case for NAB1 ( Fig.…”

Section: Cys-226 Of the Lhcii Translation Regulator Nab1 Is A Potentimentioning

confidence: 99%

“…Indeed, most protein nitrosothiols (75 to 80%) were shown to be susceptible to reduction by GSH. For example, denitrosylation of Arabidopsis GAPC1 was found to be specifically performed by GSH and to be directly controlled by the [GSH]/[GSNO] ratio but independent from the [GSH]/ [GSSG] ratio (Zaffagnini et al, 2013b). The nitrosothiols that are resistant to GSH are reduced by specific denitrosylases, the most prominent being cytosolic and mitochondrial thioredoxins, which were shown to denitrosylate numerous proteins (Benhar et al, 2010;Sengupta and Holmgren, 2013).…”

Section: Nitrosylation Of Cys-226 Acts As a Redox Switch For Fine-tunmentioning

confidence: 99%

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A light switch based on protein S-nitrosylation fine-tunes photosynthetic light-harvesting in the microalga Chlamydomonas reinhardtii

Berger¹,

Mia²,

Morisse³

et al. 2016

Plant Physiol.

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Photosynthetic eukaryotes are challenged by a fluctuating light supply, demanding for a modulated expression of nucleus-encoded light-harvesting proteins associated with photosystem II (LHCII) to adjust light-harvesting capacity to the prevailing light conditions. Here, we provide clear evidence for a regulatory circuit that controls cytosolic LHCII translation in response to light quantity changes. In the green unicellular alga Chlamydomonas reinhardtii, the cytosolic RNA-binding protein NAB1 represses translation of certain LHCII isoform mRNAs. Specific nitrosylation of Cys-226 decreases NAB1 activity and could be demonstrated in vitro and in vivo. The less active, nitrosylated form of NAB1 is found in cells acclimated to limiting light supply, which permits accumulation of lightharvesting proteins and efficient light capture. In contrast, elevated light supply causes its denitrosylation, thereby activating the repression of light-harvesting protein synthesis, which is needed to control excitation pressure at photosystem II. Denitrosylation of recombinant NAB1 is efficiently performed by the cytosolic thioredoxin system in vitro. To our knowledge, NAB1 is the first example of stimulus-induced denitrosylation in the context of photosynthetic acclimation. By identifying this novel redox cross-talk pathway between chloroplast and cytosol, we add a new key element required for drawing a precise blue print of the regulatory network of light harvesting.

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Mechanisms of Nitrosylation and Denitrosylation of Cytoplasmic Glyceraldehyde-3-phosphate Dehydrogenase from Arabidopsis thaliana

Cited by 106 publications

References 94 publications

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

S-Sulfhydration: A Cysteine Posttranslational Modification in Plant Systems

A light switch based on protein S-nitrosylation fine-tunes photosynthetic light-harvesting in the microalga Chlamydomonas reinhardtii

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