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hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorDAL SANTO, Sylvia
hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorSTAMPFL, Hansjörg
hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorKRASENSKY, Julia
hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorKEMPA, Stefan
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGIBON, Yves
hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorPETUTSCHNIG, Elena
hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorROZHON, Wilfried
hal.structure.identifierResearch Institute of Molecular Pathology [IMP]
dc.contributor.authorHEUCK, Alexander
hal.structure.identifierResearch Institute of Molecular Pathology [IMP]
dc.contributor.authorCLAUSEN, Tim
hal.structure.identifierGregor Mendel Institute of Molecular Plant Biology [GMI]
dc.contributor.authorJONAK, Claudia
dc.date.issued2012
dc.identifier.issn1040-4651
dc.description.abstractEnDiverse stresses such as high salt conditions cause an increase in reactive oxygen species (ROS), necessitating a redox stress response. However, little is known about the signaling pathways that regulate the antioxidant system to counteract oxidative stress. Here, we show that a Glycogen Synthase Kinase3 from Arabidopsis thaliana (ASK alpha) regulates stress tolerance by activating Glc-6-phosphate dehydrogenase (G6PD), which is essential for maintaining the cellular redox balance. Loss of stress-activated ASK alpha leads to reduced G6PD activity, elevated levels of ROS, and enhanced sensitivity to salt stress. Conversely, plants overexpressing ASK alpha have increased G6PD activity and low levels of ROS in response to stress and are more tolerant to salt stress. ASK alpha stimulates the activity of a specific cytosolic G6PD isoform by phosphorylating the evolutionarily conserved Thr-467, which is implicated in cosubstrate binding. Our results reveal a novel mechanism of G6PD adaptive regulation that is critical for the cellular stress response.
dc.language.isoen
dc.publisherAmerican Society of Plant Biologists (ASPB)
dc.title.enStress-induced GSK3 regulates the redox stress response by phosphorylating glucose-6-phosphate dehydrogenase in <em>Arabidopsis</em>
dc.typeArticle de revue
dc.identifier.doi10.1105/tpc.112.101279
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
bordeaux.journalThe Plant cell
bordeaux.page3380-3392
bordeaux.volume24
bordeaux.issue8
bordeaux.peerReviewedoui
hal.identifierhal-02647870
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02647870v1
bordeaux.COinSctx_ver=Z39.88-2004&amp;rft_val_fmt=info:ofi/fmt:kev:mtx:journal&amp;rft.jtitle=The%20Plant%20cell&amp;rft.date=2012&amp;rft.volume=24&amp;rft.issue=8&amp;rft.spage=3380-3392&amp;rft.epage=3380-3392&amp;rft.eissn=1040-4651&amp;rft.issn=1040-4651&amp;rft.au=DAL%20SANTO,%20Sylvia&amp;STAMPFL,%20Hansj%C3%B6rg&amp;KRASENSKY,%20Julia&amp;KEMPA,%20Stefan&amp;GIBON,%20Yves&amp;rft.genre=article


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