Identification of novel PAMP-triggered phosphorylation and dephosphorylation events in arabidopsis thaliana by quantitative phosphoproteomic analysis

Handle URI:
http://hdl.handle.net/10754/563487
Title:
Identification of novel PAMP-triggered phosphorylation and dephosphorylation events in arabidopsis thaliana by quantitative phosphoproteomic analysis
Authors:
Rayapuram, Naganand; Bonhomme, Ludovic; Bigeard, Jean; Haddadou, Kahina; Przybylski, Cédric; Hirt, Heribert ( 0000-0003-3119-9633 ) ; Pflieger, Delphine
Abstract:
Signaling 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.
KAUST Department:
Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program
Publisher:
American Chemical Society (ACS)
Journal:
Journal of Proteome Research
Issue Date:
4-Apr-2014
DOI:
10.1021/pr401268v
PubMed ID:
24601666
Type:
Article
ISSN:
15353893
Sponsors:
D.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,
Appears in Collections:
Articles; Bioscience Program; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorRayapuram, Nagananden
dc.contributor.authorBonhomme, Ludovicen
dc.contributor.authorBigeard, Jeanen
dc.contributor.authorHaddadou, Kahinaen
dc.contributor.authorPrzybylski, Cédricen
dc.contributor.authorHirt, Heriberten
dc.contributor.authorPflieger, Delphineen
dc.date.accessioned2015-08-03T11:52:41Zen
dc.date.available2015-08-03T11:52:41Zen
dc.date.issued2014-04-04en
dc.identifier.issn15353893en
dc.identifier.pmid24601666en
dc.identifier.doi10.1021/pr401268ven
dc.identifier.urihttp://hdl.handle.net/10754/563487en
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.en
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,en
dc.publisherAmerican Chemical Society (ACS)en
dc.subjectArabidopsisen
dc.subjectelectron transfer dissociationen
dc.subjectflagellinen
dc.subjectMAP kinaseen
dc.subjectpathogenen
dc.subjectphosphoproteomicsen
dc.titleIdentification of novel PAMP-triggered phosphorylation and dephosphorylation events in arabidopsis thaliana by quantitative phosphoproteomic analysisen
dc.typeArticleen
dc.contributor.departmentCenter for Desert Agricultureen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.identifier.journalJournal of Proteome Researchen
dc.contributor.institutionCNRS, UMR 8587, F-91025 Evry, Franceen
dc.contributor.institutionUEVE, LAMBE, F-91025 Evry, Franceen
dc.contributor.institutionUniv Evry Val dEssonne, CNRS, INRA, URGV Plant Genom, F-91057 Evry, Franceen
kaust.authorHirt, Heriberten

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