Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MPK phosphorylation of CDKC - Modulation of RNA polymerase II phosphorylation downstream of pathogen perception orchestrates plant immunity

ABSTRACT: phosphorylation site mapping of CDKC proteins, which were phosphorylated by MPK3 or MPK6

INSTRUMENT(S): LTQ Orbitrap

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

TISSUE(S): Diploid Cell

SUBMITTER: Sixue Chen

LAB HEAD: Sixue Chen

PROVIDER: PXD001177 | Pride | 2019-06-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Modulation of RNA polymerase II phosphorylation downstream of pathogen perception orchestrates plant immunity.

Li Fangjun F Cheng Cheng C Cui Fuhao F de Oliveira Marcos V V MV Yu Xiao X Meng Xiangzong X Intorne Aline C AC Babilonia Kevin K Li Maoying M Li Bo B Chen Sixue S Ma Xianfeng X Xiao Shunyuan S Zheng Yi Y Fei Zhangjun Z Metz Richard P RP Johnson Charles D CD Koiwa Hisashi H Sun Wenxian W Li Zhaohu Z de Souza Filho Gonçalo A GA Shan Libo L He Ping P

Cell host & microbe 20141126 6

Perception of microbe-associated molecular patterns (MAMPs) elicits host transcriptional reprogramming as part of the immune response. Although pathogen perception is well studied, the signaling networks orchestrating immune gene expression remain less clear. In a genetic screen for components involved in the early immune gene transcription reprogramming, we identified Arabidopsis RNA polymerase II C-terminal domain (CTD) phosphatase-like 3 (CPL3) as a negative regulator of immune gene expressio ...[more]

PMID: 25464831

Similar Datasets

Modulation of RNA polymerase II phosphorylation downstream of pathogen perception orchestrates plant immunity.

Project description: Not available

| S-EPMC4268009 | biostudies-literature

MKK4/5-MPK3/6 cascade regulates Agrobacterium-mediated transformation by modulating plant immunity in Arabidopsis

Project description:Agrobacterium tumefaciens is a special plant pathogen causing crown gall disease. This pathogen is well known for the technology Agrobacterium-mediated transformation. As a pathogen, Agrobacterium triggers plant immunity, and this affects transformation. But the signaling components and pathways in plant immunity to Agrobacterium remain elusive. We demonstrate two Arabidopsis MAPKKs MKK4/MKK5 and their downstream MAPKs MPK3/MPK6 play a major role in both Agrobacterium-triggered immunity and Agrobacterium-mediated transformation. Agrobacteria induce MPK3/MPK6 activity and plant defense responsive genes expression in a very early stage. This process is dependent on MKK4/MKK5 function. Loss of function of MKK4 and MKK5 or their downstream MPK3 and MPK6 abolishes plant immunity to agrobacteria, and increases the transformation frequency, while activation of MKK4 and MKK5 enhances the plant immunity and represses the transformation. Global transcriptome indicates agrobacteria induce various plant defense pathways, including ROS production, ethylene and SA-mediated defense responses, and MKK4/MKK5 is essential for these pathways induction. Activation of MKK4 and MKK5 promotes ROS production and cell death in agrobacteria infection process. Ethylene and SA act bypass of MKK4/MKK5 signaling to regulate transformation. Based on these results, we propose MKK4/5-MPK3/6 cascade is an essential signaling pathway to regulate Agrobacterium-mediated transformation by modulating Agrobacterium-triggered plant immunity.

2021-10-20 | GSE179628 | GEO

Role of MPK4 in pathogen-associated molecular pattern-triggered alternative splicing in Arabidopsis

Project description:Alternative splicing (AS) of pre-mRNAs in plants is an important mechanism of gene regulation in environmental stress tolerance but plant signals involved are essentially unknown. Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) is mediated by mitogen-activated protein kinases and the majority of PTI defense genes are regulated by MPK3, MPK4 and MPK6. These responses have been mainly analyzed at the transcriptional level, however many splicing factors are direct targets of MAPKs. Here, we studied alternative splicing induced by the PAMP flagellin in Arabidopsis.

2020-03-03 | GSE146189 | GEO

MicroRNA microarray in atmpk3 and atmpk6 Arabidopsis mutants

Project description:MicroRNA microarray profiling was performed in Arabidopsis seedlings - Col-0, atmpk3 and atmpk6 mutants to uncover the roles of MPK3 and MPK6 in microRNA biogenesis pathway.

2015-03-31 | E-MTAB-3404 | biostudies-arrayexpress

Analysis of flg22-induced transcriptional changes in mpk3, mpk4 and mpk6 mutants. - 2 weeks old seedlings compared for transcriptome after a 30min mock or 1µM flg22 treatment.

Project description:inra12-05_mut_flg_ii-FLG-MPKs ra12-05_mut_flg_ii - inra12-05_mut_flg_ii - Analysis of flg22-induced transcriptional changes in mpk3, mpk4 and mpk6 mutants. - 2 weeks old seedlings compared for transcriptome after a 30min mock or 1µM flg22 treatment.

2014-06-16 | GSE52587 | GEO

Analysis of flg22-induced transcriptional changes in mpk3, mpk4 and mpk6 mutants. - 2 weeks old seedlings compared for transcriptome after a 30min mock or 1ÂµM flg22 treatment.

2014-06-16 | E-GEOD-52587 | biostudies-arrayexpress

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

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

2021-07-23 | PXD027365 | Pride

Shared and specific targets of Arabidopsis immune MAPKs

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.

2017-12-06 | PXD006807 | Pride

Combined 15N-Labelling and TandemMOAC Quantifies Phosphorylation of MAP Kinase Substrates Downstream of MKK7 in Arabidopsis

Project description:Reversible protein phosphorylation is a widespread posttranslational modification that plays a key role in eukaryotic signal transduction. Due to the large dynamic range of protein abundance, low stoichiometry and transient nature of protein phosphorylation, the detection and accurate quantification of substrate phosphorylation by protein kinases remains a challenge. Here, we combine tandem metal-oxide affinity chromatography (tandemMOAC) with stable isotope 15N metabolic labeling for the mass spectrometry measurement and accurate quantification of low abundant, transiently phosphorylated peptides. Since tandemMOAC is not biased towards the enrichment of acidophilic, basophilic or proline-directed kinase substrates, the method is applicable to identify targets of members of all three classes of protein kinases. Using this phosphoproteomics approach, we identified several mitogen-activated protein kinase (MPK) substrates downstream of the MKK7-MPK3/6 phosphorylation cascade of Arabidopsis. The MKK7-MPK3/6 module is involved in the regulation of plant development and plant basal and systemic immune responses but little is known about downstream cascade components. The identification and validation of dynamin-related protein (DRP) 2 as a novel phosphorylation substrate of the MKK7-MPK3/6 module establishes a novel link between MPK signaling and clathrin-mediated vesicle trafficking.

2018-01-02 | PXD008200 | Pride