Quantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MPK3, MPK4 and MPK6
Alhoraibi, Hanna Mohsen Abdulrab
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Plant Science Program
Desert Agriculture Initiative
Permanent link to this recordhttp://hdl.handle.net/10754/626241
MetadataShow full item record
AbstractIn 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.
CitationRayapuram 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.
SponsorsThis 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.
JournalMolecular & Cellular Proteomics
- Determination of primary sequence specificity of Arabidopsis MAPKs MPK3 and MPK6 leads to identification of new substrates.
- Authors: Sörensson C, Lenman M, Veide-Vilg J, Schopper S, Ljungdahl T, Grøtli M, Tamás MJ, Peck SC, Andreasson E
- Issue date: 2012 Sep 1
- Functional analysis of Arabidopsis immune-related MAPKs uncovers a role for MPK3 as negative regulator of inducible defences.
- Authors: Frei dit Frey N, Garcia AV, Bigeard J, Zaag R, Bueso E, Garmier M, Pateyron S, de Tauzia-Moreau ML, Brunaud V, Balzergue S, Colcombet J, Aubourg S, Martin-Magniette ML, Hirt H
- Issue date: 2014 Jun 30
- A chemical genetic approach demonstrates that MPK3/MPK6 activation and NADPH oxidase-mediated oxidative burst are two independent signaling events in plant immunity.
- Authors: Xu J, Xie J, Yan C, Zou X, Ren D, Zhang S
- Issue date: 2014 Jan
- Arabidopsis MPK3 and MPK6 play different roles in basal and oligogalacturonide- or flagellin-induced resistance against Botrytis cinerea.
- Authors: Galletti R, Ferrari S, De Lorenzo G
- Issue date: 2011 Oct
- Mitogen-activated protein kinase 3 and 6 regulate Botrytis cinerea-induced ethylene production in Arabidopsis.
- Authors: Han L, Li GJ, Yang KY, Mao G, Wang R, Liu Y, Zhang S
- Issue date: 2010 Oct