2017
DOI: 10.1016/j.bbrc.2017.10.090
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Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues

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Cited by 36 publications
(19 citation statements)
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“…Our data underscore the complexity of redox regulation in the biochemically intricate environment of the plant cell. They add to studies implicating changes of GSNOR activities in response to stress conditions such as MV, exogenous H 2 O 2 , nitrogen stress, and hypoxia, conditions in which redox‐based modification of the protein has previously been described (Chen et al, ; Frungillo et al, ; Kovacs et al, ; Tichá et al, ; Zhan et al, ). Although we note in previous reports that GSNOR1 activity may be inhibited by H 2 O 2 in vitro (Kovacs et al, ; Tichá et al, ), such effects may be counteracted in cat2 by up‐regulation of the amount of GSNOR1 protein (Figure ) or simply not operative because H 2 O 2 accumulation inside the cell is restricted to localized subcellular areas, transient in nature, and unlikely to greatly exceed values of about 10 μM (Han et al, ; Mhamdi et al, ; Rahantaniaina et al, ; Tuzet et al, ; Xu, Guerra, Lee, & Vierling, ).…”
Section: Discussionmentioning
confidence: 93%
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“…Our data underscore the complexity of redox regulation in the biochemically intricate environment of the plant cell. They add to studies implicating changes of GSNOR activities in response to stress conditions such as MV, exogenous H 2 O 2 , nitrogen stress, and hypoxia, conditions in which redox‐based modification of the protein has previously been described (Chen et al, ; Frungillo et al, ; Kovacs et al, ; Tichá et al, ; Zhan et al, ). Although we note in previous reports that GSNOR1 activity may be inhibited by H 2 O 2 in vitro (Kovacs et al, ; Tichá et al, ), such effects may be counteracted in cat2 by up‐regulation of the amount of GSNOR1 protein (Figure ) or simply not operative because H 2 O 2 accumulation inside the cell is restricted to localized subcellular areas, transient in nature, and unlikely to greatly exceed values of about 10 μM (Han et al, ; Mhamdi et al, ; Rahantaniaina et al, ; Tuzet et al, ; Xu, Guerra, Lee, & Vierling, ).…”
Section: Discussionmentioning
confidence: 93%
“…Recent studies revealed that NO represses GSNOR activity through direct posttranslational modification of Cys residues (Frungillo et al, ; Guerra et al, ; Tichá et al, ), prompting us to test if the inhibition of GSNOR activity in cat2 pad2 was mediated by S ‐nitrosation of GSNOR1. For this, an NO fluorescent assay and the BST were employed.…”
Section: Resultsmentioning
confidence: 99%
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“…The resulting GSSG is then reduced again to GSH by the NADPH‐dependent reaction catalyzed by GR (Fatma et al ). GSNOR participates in regulation of ROS and generation of reactive nitrogen species (RNS) activation within the antioxidant system, the cellular redox status, induction of stress‐responsive genes, and stress‐induced death of entire plants (Tichá et al , Cheng et al ). Alterations in the GSH pools could have important implications in cellular redox status with impact on various cell signaling pathways (Vivancos et al ).…”
Section: Discussionmentioning
confidence: 99%
“…GSNO is metabolized to oxidized glutathione disulfide and ammonia by cysteine‐rich GSNO reductases (GSNORs), which regulate development and defense (Kwon et al, ; Leterrier et al, ; Xu, Guerra, Lee, & Vierling, ). A GSNO reductase is itself a target for S‐nitrosylation, thus representing an autoregulatory loop (Guerra, Ballard, Truebridge, & Vierling, ; Tichá, Lochman, Činčalová, Luhová, & Petřivalský, ; Zhan et al, ). Another redox mechanism, based on the action of thioredoxins such as TRX h3 and h5, reducing S‐nitrosylated proteins seems to be also relevant to control S‐nitrosylation‐related signaling specifically in plant immunity to pathogens (Kneeshaw, Gelineau, Tada, Loake, & Spoel, ; Tada et al, ).…”
Section: Relevant No Synthesis Pathways In Plantsmentioning
confidence: 99%