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dc.contributor.authorRayapuram, Naganand
dc.contributor.authorBonhomme, Ludovic
dc.contributor.authorBigeard, Jean
dc.contributor.authorHaddadou, Kahina
dc.contributor.authorPrzybylski, Cédric
dc.contributor.authorHirt, Heribert
dc.contributor.authorPflieger, Delphine
dc.date.accessioned2015-08-03T11:52:41Z
dc.date.available2015-08-03T11:52:41Z
dc.date.issued2014-03-17
dc.identifier.issn15353893
dc.identifier.pmid24601666
dc.identifier.doi10.1021/pr401268v
dc.identifier.urihttp://hdl.handle.net/10754/563487
dc.description.abstractSignaling cascades rely strongly on protein kinase-mediated substrate phosphorylation. Currently a major challenge in signal transduction research is to obtain high confidence substrate phosphorylation sites and assign them to specific kinases. In response to bacterial flagellin, a pathogen-associated molecular pattern (PAMP), we searched for rapidly phosphorylated proteins in Arabidopsis thaliana by combining multistage activation (MSA) and electron transfer dissociation (ETD) fragmentation modes, which generate complementary spectra and identify phosphopeptide sites with increased reliability. Of a total of 825 phosphopeptides, we identified 58 to be differentially phosphorylated. These peptides harbor kinase motifs of mitogen-activated protein kinases (MAPKs) and calcium-dependent protein kinases (CDPKs), as well as yet unknown protein kinases. Importantly, 12 of the phosphopeptides show reduced phosphorylation upon flagellin treatment. Since protein abundance levels did not change, these results indicate that flagellin induces not only various protein kinases but also protein phosphatases, even though a scenario of inhibited kinase activity may also be possible. © 2014 American Chemical Society.
dc.description.sponsorshipD.P. thanks the Agence Nationale pour la Recherche (ANR) for the funding ANR-2010-JCJC-1608. This work was supported by the CNRS, Genopole-France, Institut National de la Recherche Agronomique, Universite d'Evry Val d'Essonne and Region Ile-de-France. We are also indebted to Benoit Valot, Edlira Nano, Olivier Langella, and Michel Zivy for help with using MassChroQ,
dc.publisherAmerican Chemical Society (ACS)
dc.subjectArabidopsis
dc.subjectelectron transfer dissociation
dc.subjectflagellin
dc.subjectMAP kinase
dc.subjectpathogen
dc.subjectphosphoproteomics
dc.titleIdentification of novel PAMP-triggered phosphorylation and dephosphorylation events in arabidopsis thaliana by quantitative phosphoproteomic analysis
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentDesert Agriculture Initiative
dc.contributor.departmentPlant Science
dc.contributor.departmentPlant Science Program
dc.identifier.journalJournal of Proteome Research
dc.contributor.institutionCNRS, UMR 8587, F-91025 Evry, France
dc.contributor.institutionUEVE, LAMBE, F-91025 Evry, France
dc.contributor.institutionUniv Evry Val dEssonne, CNRS, INRA, URGV Plant Genom, F-91057 Evry, France
kaust.personHirt, Heribert
dc.date.published-online2014-03-17
dc.date.published-print2014-04-04


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