Chromatin phosphoproteomics unravels a function for AT-hook motif nuclear localized protein AHL13 in PAMP-triggered immunity
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ABSTRACT:
ORGANISM(S): Arabidopsis thaliana
PROVIDER: GSE119465 | GEO | 2020/12/20
REPOSITORIES: GEO
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Project description:In many eukaryotic systems during immune responses, mitogen-activated protein kinases (MAPKs) link cytoplasmic signaling to chromatin events by targeting transcription factors, chromatin remodeling complexes, and the RNA polymerase machinery. So far, knowledge on these events is scarce in plants and no attempts have been made to focus on phosphorylation events of chromatin-associated proteins. Here we carried out chromatin phosphoproteomics upon elicitor-induced activation of Arabidopsis The events in WT were compared with those in mpk3, mpk4, and mpk6 mutant plants to decipher specific MAPK targets. Our study highlights distinct signaling networks involving MPK3, MPK4, and MPK6 in chromatin organization and modification, as well as in RNA transcription and processing. Among the chromatin targets, we characterized the AT-hook motif containing nuclear localized (AHL) DNA-binding protein AHL13 as a substrate of immune MAPKs. AHL13 knockout mutant plants are compromised in pathogen-associated molecular pattern (PAMP)-induced reactive oxygen species production, expression of defense genes, and PAMP-triggered immunity. Transcriptome analysis revealed that AHL13 regulates key factors of jasmonic acid biosynthesis and signaling and affects immunity toward Pseudomonas syringae and Botrytis cinerea pathogens. Mutational analysis of the phosphorylation sites of AHL13 demonstrated that phosphorylation regulates AHL13 protein stability and thereby its immune functions.
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Project description:Mitogen-activated protein kinases constitute essential signaling mechanisms linking external signal perception to gene expression in all eukaryotes. In Arabidopsis, MAPKs are found in the cytoplasmic and nuclear compartments, but no nuclear phosphoproteomic studies of mapk mutants were performed so far. In this work, we report a panel of nuclear and chromatin-associated targets by performing phosphoproteome analyses of wild-type and mpk3, mpk4, and mpk6 mutant plants. Since the three MAPKs play a role in cell division, development and innate immunity, we also analyzed the phosphoproteomes following microbe-associated molecular pattern (MAMP) treatment. A total of 165 proteins were identified to be differentially phosphorylated when compared between genotypes and in response to MAMP treatment. Using different criteria, including different biochemical and interaction assays, a number of the putative MAPK substrates were validated as true substrates for different MAPKs. Signaling networks for the three MAPKs revealed their common role in RNA transcription, RNA processing and chromatin organization, but also specific roles in development and organelle organization. Overall, this study unravels a set of chromatin-associated targets for these three MAPKs and promises novel insights into yet undiscovered domains linking MAPK signaling to a number of chromatin-related events.
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Project description:Chromatin phosphoproteomics unravels a function for AT-hook motif nuclear localized protein AHL13 in PAMP-triggered immunity
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Project description:MAPKs are a family of highly conserved serine/threonine protein kinases that link upstream receptors to their downstream targets which can be localized in the cytoplasm or the nucleus. Pathogens produce pathogen-associated molecular patterns (PAMPs) that trigger the activation of MAPK cascades in plants. Phosphoproteomic analysis of PAMP-induced Arabidopsis plants led to the identification of several putative MAPK targets. WLIM2A is a putative phosphorylation target of MAPKs, but so far little is known about the function of WLIM2A in plant immunity. We investigated the role of WLIM2A in immunity via a reverse-genetics approach generating wlim2a knockout lines using CRISPR-Cas9, as well as complementation and phosphosite mutated WLIM2A expression lines in the wlim2a background. The wlim2a lines were compromised in their response to Pst DC3000 but showed enhanced resistance to fungal infection by Botrytis cinereae. Transcriptome analyses revealed that immune hormone signaling and biosynthesis genes of salicylic acid (SA), jasmonic acid (JA) and ethylene (ET) are differentially regulated in the wlim2a knockout lines. Pathogen assays with Pst DC3000 showed altered stomatal phenotypes in wlim2a mutants. Importantly, WLIM2A phosphomutants had opposing stomatal behaviour and resistance phenotypes in response to Pst DC3000 infection. Overall, these data show that WLIM2A is a MAPK target and that phosphorylation of WLIM2A regulates stomatal immunity.
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