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

Handle URI:
http://hdl.handle.net/10754/626241
Title:
Quantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MPK3, MPK4 and MPK6
Authors:
Rayapuram, Naganand; Bigeard, Jean; Alhoraibi, Hanna Mohsen Abdulrab; Bonhomme, Ludovic; Hesse, Anne-Marie; Vinh, Joelle; Hirt, Heribert ( 0000-0003-3119-9633 ) ; Pflieger, Delphine
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Plant Science Program; Desert Agriculture Initiative
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.
Publisher:
American Society for Biochemistry & Molecular Biology (ASBMB)
Journal:
Molecular & Cellular Proteomics
Issue Date:
23-Nov-2017
DOI:
10.1074/mcp.ra117.000135
Type:
Article
ISSN:
1535-9476; 1535-9484
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.
Additional Links:
http://www.mcponline.org/content/early/2017/11/22/mcp.RA117.000135
Appears in Collections:
Articles; Bioscience Program; Plant Science Program; Desert Agriculture Initiative; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorRayapuram, Nagananden
dc.contributor.authorBigeard, Jeanen
dc.contributor.authorAlhoraibi, Hanna Mohsen Abdulraben
dc.contributor.authorBonhomme, Ludovicen
dc.contributor.authorHesse, Anne-Marieen
dc.contributor.authorVinh, Joelleen
dc.contributor.authorHirt, Heriberten
dc.contributor.authorPflieger, Delphineen
dc.date.accessioned2017-11-29T11:13:56Z-
dc.date.available2017-11-29T11:13:56Z-
dc.date.issued2017-11-23en
dc.identifier.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.en
dc.identifier.issn1535-9476en
dc.identifier.issn1535-9484en
dc.identifier.doi10.1074/mcp.ra117.000135en
dc.identifier.urihttp://hdl.handle.net/10754/626241-
dc.description.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.en
dc.description.sponsorshipThis 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.en
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)en
dc.relation.urlhttp://www.mcponline.org/content/early/2017/11/22/mcp.RA117.000135en
dc.rightsArchived with thanks to Molecular & Cellular Proteomics. Other parties are welcome to copy, distribute, transmit and adapt the work — at no cost and without permission — for noncommercial use as long as they attribute the work to the original source using the citation above.en
dc.subjectArabidopsisen
dc.subjectSignalingen
dc.subjectMAPKen
dc.subjectImmunityen
dc.subjectPhosphoproteomeen
dc.subjectSignal Transduction*en
dc.subjectPlant Biology*en
dc.subjectProtein Kinases*en
dc.titleQuantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MPK3, MPK4 and MPK6en
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentPlant Science Programen
dc.contributor.departmentDesert Agriculture Initiativeen
dc.identifier.journalMolecular & Cellular Proteomicsen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionINRA.en
dc.contributor.institutionINRA-UBP, France.en
dc.contributor.institutioniRTSV/BGE/EDyP, CEA, France.en
dc.contributor.institutionESPCI-Paris-Tech, SMBP.en
dc.contributor.institutionCEA, BIG-BGE-EDyP, U1038 Inserm/CEA/UGA FR CNRS 3425, 38000 Grenoble, France.en
kaust.authorRayapuram, Nagananden
kaust.authorAlhoraibi, Hanna Mohsen Abdulraben
kaust.authorHirt, Heriberten
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