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dc.contributor.authorYip Delormel, Tiffany
dc.contributor.authorAvila-Ospina, Liliana
dc.contributor.authorDavanture, Marlène
dc.contributor.authorZivy, Michel
dc.contributor.authorLang, Julien
dc.contributor.authorValentin, Nicolas
dc.contributor.authorRayapuram, Naganand
dc.contributor.authorHirt, Heribert
dc.contributor.authorColcombet, Jean
dc.contributor.authorBoudsocq, Marie
dc.date.accessioned2021-11-30T07:18:53Z
dc.date.available2021-11-30T07:18:53Z
dc.date.issued2021-11-17
dc.date.submitted2021-09-09
dc.identifier.citationYip Delormel, T., Avila-Ospina, L., Davanture, M., Zivy, M., Lang, J., Valentin, N., … Boudsocq, M. (2022). In vivo identification of putative CPK5 substrates in Arabidopsis thaliana. Plant Science, 314, 111121. doi:10.1016/j.plantsci.2021.111121
dc.identifier.issn1873-2259
dc.identifier.issn0168-9452
dc.identifier.doi10.1016/j.plantsci.2021.111121
dc.identifier.urihttp://hdl.handle.net/10754/673838
dc.description.abstractCalcium signaling mediates most developmental processes and stress responses in plants. Among plant calcium sensors, the calcium-dependent protein kinases display a unique structure harboring both calcium sensing and kinase responding activities. AtCPK5 is an essential member of this family in Arabidopsis that regulates immunity and abiotic stress tolerance. To understand the underlying molecular mechanisms, we implemented a biochemical approach to identify in vivo substrates of AtCPK5. We generated transgenic lines expressing a constitutively active form of AtCPK5 under the control of a dexamethasone-inducible promoter. Lines expressing a kinase-dead version were used as a negative control. By comparing the phosphoproteome of the kinase-active and kinase-dead lines upon dexamethasone treatment, we identified 5 phosphopeptides whose abundance increased specifically in the kinase-active lines. Importantly, we showed that all 5 proteins were phosphorylated in vitro by AtCPK5 in a calcium-dependent manner, suggesting that they are direct targets of AtCPK5. We also detected several interaction patterns between the kinase and the candidates in the cytosol, membranes or nucleus, consistent with the ubiquitous localization of AtCPK5. Finally, we further validated the two phosphosites S245 and S280 targeted by AtCPK5 in the E3 ubiquitin ligase ATL31. Altogether, those results open new perspectives to decipher AtCPK5 biological functions.
dc.description.sponsorshipThis work was supported by the Agence Nationale de la Recherche to M.B. (ANR-15-CE20-0003-01) and the Ministère de l'Enseignement Supérieur et de la Recherche to T.Y.D. (MERS, doctoral grant). The IPS2 benefits from the support of the LabEx Saclay Plant Sciences-SPS (ANR-10-LABX-0040-SPS).
dc.publisherElsevier BV
dc.relation.urlhttps://linkinghub.elsevier.com/retrieve/pii/S0168945221003174
dc.rightsNOTICE: this is the author’s version of a work that was accepted for publication in Plant Science. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Plant Science, [314, , (2021-11-17)] DOI: 10.1016/j.plantsci.2021.111121 . © 2021. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.titleIn vivo identification of putative CPK5 substrates in Arabidopsis thaliana
dc.typeArticle
dc.contributor.departmentBiological and Environmental Science and Engineering (BESE) Division
dc.contributor.departmentCenter for Desert Agriculture
dc.contributor.departmentHirt Lab
dc.contributor.departmentPlant Science
dc.identifier.journalPlant Science
dc.rights.embargodate2023-11-17
dc.eprint.versionPost-print
dc.contributor.institutionUniversité Paris-Saclay, CNRS, INRAE, Univ Evry, Institute of Plant Sciences Paris-Saclay (IPS2), 91405 Orsay, France
dc.contributor.institutionUniversité de Paris, Institute of Plant Sciences Paris-Saclay (IPS2), 91405 Orsay, France
dc.contributor.institutionUniversité Paris-Saclay, INRAE, CNRS, AgroParisTech, Génétique Quantitative et Évolution (GQE) - Le Moulon, 91190 Gif-sur-Yvette, France
dc.identifier.volume314
dc.identifier.pages111121
kaust.personRayapuram, Naganand
kaust.personHirt, Heribert
dc.date.accepted2021-11-15
dc.identifier.eid2-s2.0-85119692500
refterms.dateFOA2021-11-30T13:40:40Z


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