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    Quantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MPK3, MPK4 and MPK6

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    Mol Cell Proteomics-2017-Rayapuram-mcp.RA117.000135.pdf
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    Type
    Article
    Authors
    Rayapuram, Naganand cc
    Bigeard, Jean
    Alhoraibi, Hanna cc
    Bonhomme, Ludovic
    Hesse, Anne-Marie
    Vinh, Joelle
    Hirt, Heribert cc
    Pflieger, Delphine cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Desert Agriculture Initiative
    Plant Science
    Plant Science Program
    Date
    2017-11-22
    Online Publication Date
    2017-11-22
    Print Publication Date
    2018-01
    Permanent link to this record
    http://hdl.handle.net/10754/626241
    
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    Abstract
    In Arabidopsis, mitogen-activated protein kinases MPK3, MPK4 and MPK6 constitute essential relays for a variety of functions including cell division, development and innate immunity. While some substrates of MPK3, MPK4 and MPK6 have been identified, the picture is still far from complete. To identify substrates of these MAPKs likely involved in cell division, growth and development we compared the phosphoproteomes of wild-type and mpk3, mpk4 and mpk6. To study the function of these MAPKs in innate immunity, we analyzed their phosphoproteomes following microbe-associated molecular pattern (MAMP) treatment. Partially overlapping substrates were retrieved for all three MAPKs, showing target specificity to one, two or all three MAPKs in different biological processes. More precisely, our results illustrate the fact that the entity to be defined as a specific or a shared substrate for MAPKs is not a phosphoprotein but a particular (S/T)P phosphorylation site in a given protein. As a whole, 152 peptides were identified to be differentially phosphorylated in response to MAMP treatment and/or when compared between genotypes and 70 of them could be classified as putative MAPK targets. Biochemical analysis of a number of putative MAPK substrates by phosphorylation and interaction assays confirmed the global phosphoproteome approach. Our study also expands the set of MAPK substrates to involve other protein kinases, including calcium-dependent (CDPK) and sugar non-fermenting (SnRK) protein kinases.
    Citation
    Rayapuram N, Bigeard J, Alhoraibi H, BONHOMME L, Hesse A-M, et al. (2017) Quantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MPK3, MPK4 and MPK6 . Molecular & Cellular Proteomics: mcp.RA117.000135. Available: http://dx.doi.org/10.1074/mcp.ra117.000135.
    Sponsors
    This work was supported by the Agence Nationale de la Recherche (ANR-2010-JCJC-1608 to D. P.) and by the King Abdullah University of Science and Technology. The IPS2 benefits from the support of the LabEx Saclay Plant Sciences-SPS (ANR-10-LABX-0040-SPS). We would like to thank Veronique Legros and Huoming Zhang for technical assistance in MS, and Christophe Bruley, Véronique Dupierris and Emmanuelle Lastrucci (EDyP) for (83)informatics support. We would like to thank Carlos Xavier Pita and Heno Hwang from KAUST for scientific Illustrations.
    Publisher
    American Society for Biochemistry & Molecular Biology (ASBMB)
    Journal
    Molecular & Cellular Proteomics
    DOI
    10.1074/mcp.ra117.000135
    PubMed ID
    29167316
    Additional Links
    http://www.mcponline.org/content/early/2017/11/22/mcp.RA117.000135
    ae974a485f413a2113503eed53cd6c53
    10.1074/mcp.ra117.000135
    Scopus Count
    Collections
    Articles; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Plant Science Program; Desert Agriculture Initiative

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