Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ABSTRACT: 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.

INSTRUMENT(S): Q Exactive

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

TISSUE(S): Root

SUBMITTER: Yuri Ohkubo

LAB HEAD: Yoshikatsu Matsubayashi

PROVIDER: PXD022343 | Pride | 2021-03-02

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Quantitative proteomic comparison between wild type Col and sec-5 mutant using 15N metabolic labeling

Project description:SECRET AGENT (SEC) is an O-GlcNAc transferase involved in O-GlcNAcylation of many proteins. However, sec-5 null allele mutant phenotype is very subtle. To examine if there are proteins that show altered expression in the sec-5 mutant compared to wild-type Col, we designed MS experiments to identify these candidates on a global scale using 15N metabolic labeling.

2022-02-04 | PXD030575 | Pride

Using targeted quantification (PRM) to quantify proteins between wild type Col and acinus-2 pinin-1 mutant with 15N metabolic labeling

Project description:ACINUS and PININ genes regulate transcription and alternative splicing (Bi et al., 2021) and we hypothesize that some proteins should have altered expression in the double mutant. Therefore, MS experiments were designed to identify these altered proteins on a global scale using 15N metabolic labeling. Some of these altered proteins were subjected to targeted quantification.

2022-04-19 | PXD030096 | Pride

Relative quantification of 15N labeled acinus-2 pinin-1 and 14N labeled Col through Data Dependent Acquisition to obtain peptide information for targeted Parallel Reaction Monitoring experiment

Project description:To examine the properties of 14N and 15N labeled peptides using Parallel Reaction Monitoring (PRM) on a high resolution, high accuracy mass spectrometer we first set up this DDA experiment. The purpose of this experiment was to choose peptides that are good candidates for targeted quantification. The retention times, mass, and charge from 42 candidate peptides were acquired for targeted quantification.

2022-06-09 | PXD030098 | Pride

Temperature induced remodeling of the photosynthetic machinery of the red alga Cyanidioschyzon merolae

Project description:Cyanidioschyzon merolae is a thermophilic red alga with an optimum growth temperature of 42°C. In this study we investigated the acclimation process of the alga to a colder temperature (25°C). To this aim we performed quantitative proteomic analyses of whole cells as well as solubilized thylakoid protein complexes.

2017-04-03 | PXD005615 | Pride

Quantitative proteomic comparison between wild type Col and acinus-2 pinin-1 mutant using 15N metabolic labeling

2022-02-04 | PXD030081 | Pride

Proteomic insights into ulvan degradation by the marine Flavobacterium Formosa agariphila

Project description:The marine Flavobacterium Formosa agariphila KMM 3901T is able to use a broad range of different carbohydrates as growth substrates. This is reflected in the strain’s repertoire of 13 polysaccharide utilization loci (PUL) in total. One PUL – termed as PUL H – is responsible for ulvan degradation, which is a widely distributed, algal-derived polysaccharide. The PUL comprises almost 40 genes, coding for transporters, lyases, glycoside hydrolases or sulfatases, among others. These proteins catalyse the breakdown of ulvan or the uptake of degradation products. A combined application of isotope labeling, subcellular protein fractionation and quantitative proteomics revealed that corresponding PUL encoded proteins were substrate specific up-regulated in ulvan-cultivated cells. The sulphated polysaccharide ulvan also induced the specific expression of proteins necessary for subsequent monosaccharide degradation. Compared to a control (fructose-cultivated cells), expression of PUL H additionally responded to rhamnose, a basic component of ulvan, indicating that this monosaccharide might signal ulvan availability in the environment. Our proteome analyses proofed a substrate specific expression of proteins involved in ulvan utilization and allowed us to deduce a comprehensive degradation pathway for this complex marine polysaccharide.

2019-07-25 | PXD009299 | Pride

SPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 2: EtHCD)

Project description:The recent discovery of SPY-catalyzed protein O-fucosylation reveals a novel mechanism for regulating nucleocytoplasmic protein functions in plants. Genetic evidence indicates important roles of SPY in diverse developmental and physiological processes, however, the upstream signal controlling SPY activity and the downstream substrate proteins O-fucosylated by SPY remain largely unknown. Here, we demonstrate that SPY mediates sugar-dependent growth. We further identify hundreds of O-fucosylated proteins using lectin affinity chromatography followed by mass spectrometry. All the O-fucosylation events quantified in proteomic analyses are undetectable or decreased in the spy mutants and thus likely catalyzed by SPY. The O-fucosylome includes mostly nuclear and cytosolic proteins. Many O-fucosylated proteins function in essential cellular processes, hormone signaling, and developmental programs, consistent with the genetic functions of SPY. The O-fucosylome also includes many proteins modified by O-linked-N-acetylglucosamine (O-GlcNAc) and by phosphorylation downstream of the target of rapamycin (TOR) kinase, revealing the convergence of these nutrient signaling pathways on key regulatory functions such as post-transcriptional/translational regulation and hormonal responses. Our study identifies numerous targets of SPY/O-fucosylation and potential nodes of crosstalk among sugar/nutrient signaling pathways, enabling future dissection of the signaling network that mediates sugar regulation of plant growth and development.

2023-05-10 | PXD038491 | Pride

SPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 1: HCD)

2023-05-10 | PXD038490 | Pride

15N Stable-isotope-labeling in Arabidopsis (SILIA) quantitative MS analysis of the AtACINUS interactome

Project description:AtACINUS protein is involved in regulation of alternative transcription and splicing(AS). Identifying interaction partners and protein complex compositions for AtACINUS can produce valuable information on the mechanisms by which they regulate transcription and AS, as well as post-translational modifications on AtACINUS. A homozygous 35S::AtACINUS-GFP/acinus-2 plant was selected for similar protein expression level to the endogenous AtACINUS protein of wild-type plants using a native α-AtACINUS antibody. We isolated putative AtACINUS interaction partners from young Arabidopsis seedlings using the native α-AtACINUS antibody. Plants expressing TAP-GFP under 35S promoter were used as controls.

2020-12-02 | PXD020700 | Pride

Proteomic comparison of Chlamydomonas wildtype and calredoxin knock-down mutants via 14N/15N metabolic labeling

Project description:Calcium (Ca2+) and redox signaling play important roles in acclimation processes from archaea to eukaryotic organisms. Herein we characterized a unique protein from Chlamydomonas reinhardtii that has the competence to integrate Ca2+- and redox-related signaling. This protein, designated as calredoxin (CRX), combines four Ca2+-binding EF-hands and a thioredoxin (TRX) domain. A crystal structure of CRX, at 1.6 Å resolution, revealed an unusual calmodulin-fold of the Ca2+-binding EF-hands, which is functionally linked via an inter-domain communication path with the enzymatically active TRX domain. CRX is chloroplast-localized and interacted with a chloroplast 2-Cys-peroxiredoxin (PRX1). Ca2+-binding to CRX is critical for its TRX activity and for efficient binding and reduction of PRX1. Thereby, CRX represents a new class of Ca2+-dependent "sensor-responder" proteins. Genetically engineered Chlamydomonas strains with strongly diminished amounts of CRX revealed altered photosynthetic electron transfer and were affected in oxidative stress response underpinning a function of CRX in stress acclimation.

2016-10-12 | PXD003759 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data