Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Methionine metabolism regulates T cell fate by KCa3.1 activity (RNA-Seq)

ABSTRACT: We found that methionine availibility during T cell activation regulates rapid NFAT1 activation, thereby governing T cell fate. Further, acute methionine limitation didn't affect global histone methylation status stating the crucial role of methioinine during early TCR activation.

ORGANISM(S): Mus musculus

PROVIDER: GSE221235 | GEO | 2025/05/30

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Methionine metabolism regulates T cell fate by KCa3.1 activity (ATAC-Seq)

Project description:We found that methionine availibility during T cell activation regulates rapid NFAT1 activation, thereby governing T cell fate. Further, acute methionine limitation didn't affect global histone methylation status stating the crucial role of methioinine during early TCR activation.

2025-06-11 | GSE299550 | GEO

Methionine metabolism regulates T cell fate by KCa3.1 activity (RNA-Seq)

2025-06-11 | GSE299554 | GEO

Methionine metabolism regulates T cell fate by KCa3.1 activity (Cut&Run)

2025-06-11 | GSE299551 | GEO

Methionine metabolism regulates T cell fate by KCa3.1 activity (ATAC-Seq)

2025-05-30 | GSE221236 | GEO

Methionine metabolism regulates T cell fate by KCa3.1 activity (Cut&Run)

2025-05-30 | GSE221095 | GEO

Early methionine availability attenuates T cell exhaustion

Project description:T cell receptor (TCR) activation is regulated in multifaceted ways, including niche-specific nutrient availability. We investigated how methionine (Met) availability and TCR signaling interplay in the earliest events of T cell activation to affect subsequent cell fate. Limiting Met during the initial 30 minutes of TCR engagement increased Ca2+ influx, NFAT1 (Nfatc2) activation and promoter occupancy leading to T cell exhaustion. We identified changes in the protein arginine methylome during the initial TCR engagement and discovered a novel arginine methylation of a Ca2+-activated potassium transporter, KCa3.1, which regulates Ca2+-mediated NFAT1 signaling for optimal activation. Ablation of KCa3.1 arginine methylation increased NFAT1 nuclear localization, rendering T cells dysfunctional in murine tumour and infection models. Furthermore, acute Met supplementation at early stages reduced nuclear NFAT1 in tumour-infiltrating T cells and augmented their anti-tumour activity. Our findings identify a metabolic event occurring early after T cell activation that influences cell fate.

2025-05-29 | GSE221350 | GEO

An early, novel arginine methylation of KCa3.1 attenuates subsequent T cell exhaustion.

Project description:We identified changes in the protein arginine methylome during the initial 30 min of TCR engagement and discovered a novel arginine methylation of a Ca2+ -activated potassium transporter, KCa3.1, which regulates Ca2+ -mediated NFAT1 signaling to ensure optimal activation.

2025-05-29 | PXD064423 | Pride

Methionine metabolism regulates T cell fate by KCa3.1 activity

Project description:Methionine metabolism regulates T cell fate by KCa3.1 activity

| PRJNA1276135 | ENA

Impact of dietary methionine, tryptophan, and niacin deficiency on gut microbiota in mice.

Project description:Emerging evidence indicates that selective nutrient restriction can reproduce metabolic benefits. Although methionine and branched-chain amino acid limitation improve metabolism and reshape the gut microbiome, the effects of other nutrients are still unclear. In this study, we examine the consequences of restricting methionine, tryptophan, and niacin, and find that their transient deprivation induces significant changes in gut microbiota.

2025-07-12 | GSE300499 | GEO

Carboxy-Methylation of PP2Ac Integrates Methionine Availability with Cancer Cell Proliferation

Project description:Cancer cells exhibit a well-documented, yet poorly understood, dependence on exogenous methionine, despite retaining the capacity to convert homocysteine to methionine. In contrast, non-tumorigenic cells can proliferate when methionine is replaced by homocysteine. To investigate the mechanistic basis of this methionine dependence, we examined how methionine metabolism impacts cell cycle progression. We identified carboxy-methylation of the catalytic subunit of Protein Phosphatase 2A (PP2A) as a critical node linking methionine availability to proliferation. PP2A methylation was found to be highly sensitive to intracellular S-adenosylmethionine (SAM) levels, with reduced methylation correlating with impaired proliferation under methionine restriction. Overexpression of Protein Phosphatase Methylesterase-1 (PME-1), which demethylates PP2A, or expression of a Leu309-deleted PP2A mutant that mimics the demethylated form, was sufficient to reduce proliferation even in methionine-independent cells. These findings support a model in which methionine limitation lowers SAM availability, thereby decreasing PP2A methylation and impairing cell cycle progression. Our study reveals a novel mechanistic link between methionine metabolism and the cell cycle and suggests that PP2A methylation plays a key role in the unique methionine dependence of cancer cells.

2025-07-03 | GSE301557 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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