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MPK3/6-induced degradation of ARR1/10/12 promotes salt tolerance in Arabidopsis

ABSTRACT: Here we present a LC-MS/MS analysis on ARR1/10/12-His recombinant proteins that were phosphorylated by MPK3 and MPK6 in vitro

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Zhenwei Yan

LAB HEAD: Zhaojun Ding

PROVIDER: PXD027365 | Pride | 2021-07-23

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	ARR1-MPK3.raw	Raw
	ARR1-MPK3txt.rar	Other
	ARR1-MPK6.raw	Raw
	ARR1-MPK6txt.rar	Other
	ARR10-MPK3.raw	Raw

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Project description: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 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 activation by a microbe-associated molecular pattern (MAMP). 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 finally expands the set of MAPK substrates to involve other protein kinases, including calcium-dependent (CDPK) and sugar non-fermenting (SnRK) protein kinases.

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