Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Phosphoproteomics of WT and nrt1.1 under high nitrate and low nitrate

ABSTRACT: We performed a comparative phosphoproteomic analysis of Arabidopsis root membrane proteins of WT and nrt1.1-1 under low nitrate (LN) and high nitrate (HN) availability in order to identify the downstream components that may be involved in NRT1.1-dependent LR growth and signal transduction.

INSTRUMENT(S):

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

TISSUE(S): Plant Cell, Root

SUBMITTER: Zhe Zhu

LAB HEAD: Xu Na Wu

PROVIDER: PXD048853 | Pride | 2024-02-22

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SEARCH.zip	Other
	WT-HN-MF-15min-1.raw	Raw
	WT-HN-MF-15min-2.raw	Raw
	WT-HN-MF-15min-3.raw	Raw
	WT-HN-MF-15min-4.raw	Raw

Items per page:

1 - 5 of 33

Similar Datasets

Phosphoproteome profiling under low nitrate and high nitrate in Arabisopsis wild type roots

Project description:In this project, we treated Arabidopsis wild type (Col-0) with low nitrate (0.2 mM KNO3) and high nitrate (5 mM KNO3) after nitrate starvation. Next we harvested root, and then we performed memebrane fraction and cytosolic fraction isolation for trypsin digestion and phosphopeptide enrichment.

2024-05-21 | PXD014146 | Pride

Identification of putative phosphorylation substrates of BRI1 in response to brassinolide and sucrose

Project description:Plants respond to various external and internal stimuli by activating signal transduction pathways. The plasma membrane, acting as the cell boundary, provides a platform for various signaling components. These include cell surface receptor-like kinases, intrinsic transporters, membrane-anchored proteins, and cytosolic signaling components attached to the membrane from its cytosolic side. Phosphorylation is one of the most sensitive and essential post-translational modifications. To identify the sequential kinase-target relationships and understand the triggers for downstream regulatory complexes, we employed a phosphoproteomic approach. By subjecting plants to brassinolide and/or sucrose, we aim to identify the BR-BRI1 downstream substrates and investigate the possible impact of sucrose on this signaling pathway.

2025-05-07 | PXD052599 | Pride

Nitrate Starvation time course membrane protein phosphoproteomics

Project description:Nitrate nutrtition was withdrawn from Arabiodpsis plants to study early responses upon nitrate depletion. Plants were grown under full nutrition (3mM nitrate) for three weeks and then transferred to nutrient solution without nitrate for 15 minutes and 3 hours.

2024-05-21 | PXD015390 | Pride

Phosphorylation profiling of phytocytokine versus MAMP signaling reveals systemin-specific signaling events

Project description:Plasma membrane-localized pattern recognition receptors (PRRs) percieve host-derived phytocytokines (e.g. systemin) and microbe-associated molecular patterns (MAMPs; e.g. flg22 and chitin). Upon ligand binding, activation of PRRs induces similar early phosphorylation-regulated responses including extracellular alkalization and reactive oxygen species burst. However, despite similar early signaling events, the downstream responses are distinct: MAMPs trigger plant innate immunity, and the wound response is elicited by systemin. Therefore, the question arises as to how systemin-mediated responses differ from that of MAMPs, and how specificity is achieved. Here we used a Solanum peruvianum suspension cell culture to analyze phospho-proteomic responses triggered by 20nM flg22 and 15 ug/mL chitin compared to mock(water) treatment. Samples were analyzed in a time series of 0,1,2,5,15 and 45 min after elicitor treatment in six biological replicates.Sample numbering scheme:TreatmentTimeReplicate(e.g., F153 corresponds to flg22 treatment, 15min, the 3rd biological replicate; "C" and "H" are for chitin and water-treated samples,respectively.)

2025-06-17 | PXD062081 | Pride

Phosphorylation landscape on time-resolved SYR1-dependent systemin signaling pathway

Project description:Systemin was identified in 1991 as the first plant signaling peptide, and is required for defense against insect herbivores and necrotrophic pathogens in tomato plants. Systemin was first conceived as a hormone-like, long-distance messenger mediating the activation of systemic defense responses far from the site of insect attack. It was later shown to rather act as a phytocytokine, amplifying the local wound response for production of downstream signals resulting in defense gene activation in distal tissues. Systemin perception and signaling rely on the systemin receptor SYR1. However, SYR1-dependent signaling, and how systemin signaling differs from other peptide-mediated signaling pathways, is largely unknown. Here we used a Solanum peruvianum suspension cell culture to analyze phospho-proteomic responses triggered by 10 nM systemin. Samples were analyzed in a time series of 0, 1, 2, 5, 15, and 45 min after systemin treatment. To identify systemin-specific events a mutant cell culture lacking the SYR1 systemin receptor was analyzed in parallel. The experiment was performed in six biological replicates. Samples numbering scheme: Genotype_TreatmentTimeReplicate(e.g.,WT_S53 corresponding to wild-type cells treated with systemin, for 5min, the 3rd biological replicates)

2025-06-17 | PXD054229 | Pride

nitrate induction - nlp mutants-Nitrate induction - nlp mutants

Project description:bra-inra09-02_bioen_nitrogen - nitrate induction - nlp mutants - Short term nitrate induction kinetics in wildtype, nlp7-1, nlp7-3 and nlp6nlp7 - 10 days old seedling grown in liquid culture on 3mM nitrate wer starvec for N for 3 days and the kinetic for the resupply of nitrate was studied during a short kinetic (0,5, 10,20 minutes). 26 dye-swap - gene knock out,time course

2012-12-01 | E-GEOD-39261 | biostudies-arrayexpress

Human protein phosphorylation analysis

Project description:Mycobacterium tuberculosis (Mtb) protein kinase G (PknG) is a critical protein which can inhibit the maturation of phagosome and its fusion with the lysosome, providing Mtb’s latency and survival in the host. However, its signaling pathways and functions in the human body are still unclear and needed to be further studied. In our research, we used the human protein microarray to study the proteins interacting with PknG and have found a list of proteins that are potentially related to PknG in the host, which may contribute to the infection of Mtb. Among these positive hits, we found human protein CypA has strong interaction with PknG. We further validated the interaction between PknG and CypA in vitro and in vivo and investigated its role in the infection of macrophage cells. Finally, we found that PknG can significantly down-regulate protein expression level of CypA through phosphorylation in site of T107 as well as its induction of inflammatory response through NF-κB and ERK1/2 pathways. Meanwhile, the survival of Mycobacterium smegmetis (Msm) in the macrophages with overexpressing PknG is also improved with lessen of cytokines expression. Our results provided a resourceful research base of PknG in regards to various target human proteins and offered an insightful understanding of PknG’s function in the host.

2018-10-10 | PXD009237 | Pride

Day-night phosphoproteome analysis in WT, pgm mutant and sweet11/sweet12 mutant

Project description:In this progect, we anallyzed the phosphoproteome change of shoot and root from WT pgm mutant and sweet11/sweet12 mutant at the end of day and the end of night. The purpose is to understand the role of sugar distribution in shoot and root phopshoproteome.

2022-08-12 | PXD031942 | Pride

A type 2C protein phosphatase activates high-affinity nitrate uptake by directly dephosphorylating NRT2.1 in Arabidopsis

Project description:Nitrate transporter NRT2.1, which plays a central role in high-affinity nitrate uptake in roots, is activated at the post-translational level in response to nitrogen (N) starvation. However, critical enzymes required for post-translational activation of NRT2.1 remain to be identified. Here, we show that a type 2C protein phosphatase, designated CEPD-induced phosphatase (CEPH), activates high-affinity nitrate uptake by directly dephosphorylating S501 of NRT2.1, a residue that functions as a negative phospho-switch. CEPH is predominantly expressed in epidermal and cortex cells in roots and up-regulated by N starvation via a CEPDL2/CEPD1/2-mediated long-distance signaling from shoots. Loss of CEPH leads to a marked decrease in high-affinity nitrate uptake, tissue nitrate content, and plant biomass. Collectively, our results identify CEPH as a crucial enzyme in N starvation-dependent activation of NRT2.1, providing molecular and mechanistic insights into how plants regulate high-affinity nitrate uptake at the post-translational level in response to the N environment.

2021-03-02 | PXD022343 | Pride

nitrate induction - nlp mutants-Nitrate induction - nlp mutants

2012-12-01 | GSE39261 | GEO