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Mol Cell Proteomics. 2018 Jan;17(1):61-80. doi: 10.1074/mcp.RA117.000135. Epub 2017 Nov 22.

Quantitative Phosphoproteomic Analysis Reveals Shared and Specific Targets of Arabidopsis Mitogen-Activated Protein Kinases (MAPKs) MPK3, MPK4, and MPK6.

Author information

1
From the ‡Center for Desert Agriculture, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
2
§Institute of Plant Sciences Paris-Saclay IPS2, CNRS, INRA, Université Paris-Sud, Université Evry, Université Paris-Saclay, Bâtiment 630, 91405 Orsay, France.
3
¶Institute of Plant Sciences Paris-Saclay IPS2, Paris Diderot, Sorbonne Paris-Cité, Bâtiment 630, 91405 Orsay, France.
4
‖UMR INRA/UBP Génétique, Diversité et Écophysiologie des Céréales, Université de Clermont-Ferrand, 63039 Clermont-Ferrand, France.
5
**CEA, BIG-BGE-EDyP, U1038 Inserm/CEA/UGA, 38000 Grenoble, France.
6
‡‡ESPCI Paris, PSL Research University, Spectrométrie de Masse Biologique et Protéomique (SMBP), CNRS USR 3149, 10 rue Vauquelin, F75231 Paris cedex05, France.
7
From the ‡Center for Desert Agriculture, 4700 King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia; heribert.hirt@kaust.edu.sa.
8
§§CNRS, LAMBE UMR 8587, Université d'Evry Val d'Essonne, Evry, France.

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. Although 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. One hundred fifty-two 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 nonfermenting (SnRK) protein kinases.

PMID:
29167316
PMCID:
PMC5750851
[Available on 2019-01-01]
DOI:
10.1074/mcp.RA117.000135

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