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Sustained mitogen-activated protein kinase activation reprograms defense metabolism and phosphoprotein profile in Arabidopsis thaliana

Affiliation
Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Halle/Saale, Germany
Lassowskat, Ines;
GND
129256323
Affiliation
Julius Kühn-Institute (JKI), Federal Research Centre for Cultivated Plants, Institute for Ecological Chemistry, Plant Analysis and Stored Product Protection, Berlin, Germany ; Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Halle/Saale, Germany
Böttcher, Christoph;
Affiliation
Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Halle/Saale, Germany
Eschen-Lippold, Lennart;
Affiliation
Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Halle/Saale, Germany
Scheel, Dierk;
Affiliation
Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Halle/Saale, Germany
Lee, Justin

Mitogen-activatedproteinkinases(MAPKs)targetavarietyofproteinsubstratestoregulatecellularsignalingprocessesineukaryotes.Inplants,thenumberofidentifiedMAPKsubstratesthatcontrolplantdefenseresponsesisstilllimited.Here,wegeneratedtransgenicArabidopsisthalianaplantswithaninduciblesystemtosimulateinvivoactivationoftwostress-activatedMAPKs,MPK3,andMPK6.MetabolomeanalysisrevealedthatthisartificialMPK3/6activation(withoutanyexposuretopathogensorotherstresses)issufficienttodrivetheproductionofmajordefense-relatedmetabolites,includingvariouscamalexin,indoleglucosinolateandagmatinederivatives.Anaccompanying(phospho)proteomeanalysisledtodetectionofhundredsofpotentialphosphoproteinsdownstreamofMPK3/6activation.BesidesknownMAPKsubstrates,manycandidatesonthislistpossesstypicalMAPK-targetedphosphositesandinmanycases,thecorrespondingphosphopeptidesweredetectedbymassspectrometry.Notably,severaloftheseputativephosphoproteinshavebeenreportedtobeassociatedwiththebiosynthesisofantimicrobialdefensesubstances(e.g.,WRKYtranscriptionfactorsandproteinsencodedbythegenesfromthe“PEN”pathwayrequiredforpenetrationresistancetofilamentouspathogens).Thus,thisworkprovidesaninventoryofcandidatephosphoproteins,includingputativedirectMAPKsubstrates,forfutureanalysisofMAPK-mediateddefensecontrol.(ProteomicsdataareavailablewiththeidentifierPXD001252viaProteomeXchange,http://proteomecentral.proteomexchange.org).

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