Missing links in understanding redox signaling via thiol/disulfide modulation: how is glutathione oxidized in plants?
Identifieur interne : 000741 ( Main/Exploration ); précédent : 000740; suivant : 000742Missing links in understanding redox signaling via thiol/disulfide modulation: how is glutathione oxidized in plants?
Auteurs : Marie-Sylviane Rahantaniaina [France] ; Andrée Tuzet ; Amna Mhamdi ; Graham NoctorSource :
- Frontiers in plant science [ 1664-462X ] ; 2013.
Abstract
Glutathione is a small redox-active molecule existing in two main stable forms: the thiol (GSH) and the disulphide (GSSG). In plants growing in optimal conditions, the GSH:GSSG ratio is high in most cell compartments. Challenging environmental conditions are known to alter this ratio, notably by inducing the accumulation of GSSG, an effect that may be influential in the perception or transduction of stress signals. Despite the potential importance of glutathione status in redox signaling, the reactions responsible for the oxidation of GSH to GSSG have not been clearly identified. Most attention has focused on the ascorbate-glutathione pathway, but several other candidate pathways may couple the availability of oxidants such as H2O2 to changes in glutathione and thus impact on signaling pathways through regulation of protein thiol-disulfide status. We provide an overview of the main candidate pathways and discuss the available biochemical, transcriptomic, and genetic evidence relating to each. Our analysis emphasizes how much is still to be elucidated on this question, which is likely important for a full understanding of how stress-related redox regulation might impinge on phytohormone-related and other signaling pathways in plants.
DOI: 10.3389/fpls.2013.00477
PubMed: 24324478
PubMed Central: PMC3838956
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In plants growing in optimal conditions, the GSH:GSSG ratio is high in most cell compartments. Challenging environmental conditions are known to alter this ratio, notably by inducing the accumulation of GSSG, an effect that may be influential in the perception or transduction of stress signals. Despite the potential importance of glutathione status in redox signaling, the reactions responsible for the oxidation of GSH to GSSG have not been clearly identified. Most attention has focused on the ascorbate-glutathione pathway, but several other candidate pathways may couple the availability of oxidants such as H2O2 to changes in glutathione and thus impact on signaling pathways through regulation of protein thiol-disulfide status. We provide an overview of the main candidate pathways and discuss the available biochemical, transcriptomic, and genetic evidence relating to each. Our analysis emphasizes how much is still to be elucidated on this question, which is likely important for a full understanding of how stress-related redox regulation might impinge on phytohormone-related and other signaling pathways in plants. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">24324478</PMID><DateCompleted><Year>2014</Year><Month>06</Month><Day>24</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>29</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><PubDate><Year>2013</Year><Month>Nov</Month><Day>25</Day></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Missing links in understanding redox signaling via thiol/disulfide modulation: how is glutathione oxidized in plants?</ArticleTitle><Pagination><MedlinePgn>477</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2013.00477</ELocationID><Abstract><AbstractText>Glutathione is a small redox-active molecule existing in two main stable forms: the thiol (GSH) and the disulphide (GSSG). In plants growing in optimal conditions, the GSH:GSSG ratio is high in most cell compartments. Challenging environmental conditions are known to alter this ratio, notably by inducing the accumulation of GSSG, an effect that may be influential in the perception or transduction of stress signals. Despite the potential importance of glutathione status in redox signaling, the reactions responsible for the oxidation of GSH to GSSG have not been clearly identified. Most attention has focused on the ascorbate-glutathione pathway, but several other candidate pathways may couple the availability of oxidants such as H2O2 to changes in glutathione and thus impact on signaling pathways through regulation of protein thiol-disulfide status. We provide an overview of the main candidate pathways and discuss the available biochemical, transcriptomic, and genetic evidence relating to each. Our analysis emphasizes how much is still to be elucidated on this question, which is likely important for a full understanding of how stress-related redox regulation might impinge on phytohormone-related and other signaling pathways in plants. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rahantaniaina</LastName><ForeName>Marie-Sylviane</ForeName><Initials>MS</Initials><AffiliationInfo><Affiliation>Institut de Biologie des Plantes, Université Paris-Sud Orsay, France ; Institut National de Recherche Agronomique, UMR Environnement et Grandes Cultures Thiverval-Grignon, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tuzet</LastName><ForeName>Andrée</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Mhamdi</LastName><ForeName>Amna</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Noctor</LastName><ForeName>Graham</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>11</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Plant Sci</MedlineTA><NlmUniqueID>101568200</NlmUniqueID><ISSNLinking>1664-462X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">dehydroascorbate</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathione S-transferase</Keyword><Keyword MajorTopicYN="N">hydrogen peroxide</Keyword><Keyword MajorTopicYN="N">oxidative stress</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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first="Marie-Sylviane" last="Rahantaniaina">Marie-Sylviane Rahantaniaina</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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