Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Endoplasmic reticulum protein TXNDC5 interacts with PRDX6 and HSPA9 to regulate glutathione metabolism and lipid peroxidation in hepatic AML12 cell line

ABSTRACT: Endoplasmic reticulum protein TXNDC5 interacts with PRDX6 and HSPA9 to regulate glutathione metabolism and lipid peroxidation in hepatic AML12 cell line

PROVIDER: PRJNA1011268 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR25835400_1.fastq.gz	Fastqsanger.gz
	SRR25835400_2.fastq.gz	Fastqsanger.gz
	SRR25835401_1.fastq.gz	Fastqsanger.gz
	SRR25835401_2.fastq.gz	Fastqsanger.gz
	SRR25835402_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 22

Similar Datasets

Endoplasmic reticulum protein TXNDC5 interacts with PRDX6 and HSPA9 to regulate glutathione metabolism and lipid peroxidation in hepatic AML12 cell line

Project description:The goal of this study was to determine TXNDC5 hepatic transcriptome interaction by comparing high-throughput data for KO vs. WT AML12 cells.

2023-12-27 | GSE242049 | GEO

SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [KPK_Slc33a1_KO_TUNC]

Project description:SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [KPK_Slc33a1_KO_TUNC]

| PRJNA1420681 | ENA

SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [ERIP_RNASeq]

Project description:SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [ERIP_RNASeq]

| PRJNA1420688 | ENA

SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [KPK_Slc33a1_KO_TUNC]

Project description:Endoplasmic reticulum stress and redox homeostasis influence protein folding and unfolded protein response signaling. To examine transcriptional responses associated with Slc33a1 loss and complementation, we performed RNA sequencing of KPK cells with Slc33a1 knockout and cells complemented with either empty vector or cDNA constructs. Cells were treated with either DMSO or tunicamycin to induce ER stress, and total RNA was collected for sequencing. This dataset provides transcriptome profiles that enable comparison of gene expression changes across genotypes and treatment conditions.

2026-02-12 | GSE318827 | GEO

SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis

Project description:This study investigates how loss of the ER transporter SLC33A1 affects glutathione redox balance and protein cysteine reactivity in the endoplasmic reticulum. Oxidized cysteine reactivity profiling and whole-cell proteomics were performed in Slc33a1 knockout KPK cells and cDNA-complemented controls. Quantitative TMT-based proteomics identified increased oxidation of protein disulfide isomerases and other ER-resident proteins, indicating disruption of ER redox homeostasis and proteostasis. Additional experiments examined unfolded protein response activation and genetic interactions with ER quality-control pathways. The dataset includes cysteine reactivity profiling and unenriched proteomics data acquired by LC–MS/MS and processed using standard proteomics pipelines.

2026-02-13 | PXD074382 | Pride

SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [ERIP_RNASeq]

Project description:The endoplasmic reticulum (ER) is the primary site of synthesis of secretory and membrane proteins, suggesting that specific mRNAs may be enriched at the ER surface. To characterize ER-associated transcripts, ER fractions were isolated using ER immunoprecipitation (ER-IP) and RNA was extracted from ER-bound material and whole-cell lysates. RNA sequencing was performed to compare transcript composition between ER-associated and total cellular RNA. ER-IP RNA sequencing revealed enrichment of transcripts encoding proteins localized to the plasma membrane, ER, Golgi apparatus, lysosome, and extracellular space. This dataset provides transcriptomic profiling of ER-associated RNA and corresponding whole-cell controls.

2026-02-12 | GSE318826 | GEO

Endoplasmic Reticulum Protein TXNDC5 Interacts with PRDX6 and HSPA9 to Regulate Glutathione Metabolism and Lipid Peroxidation in the Hepatic AML12 Cell Line.

Project description:Non-alcoholic fatty liver disease or steatosis is an accumulation of fat in the liver. Increased amounts of non-esterified fatty acids, calcium deficiency, or insulin resistance may disturb endoplasmic reticulum (ER) homeostasis, which leads to the abnormal accumulation of misfolded proteins, activating the unfolded protein response. The ER is the primary location site for chaperones like thioredoxin domain-containing 5 (TXNDC5). Glutathione participates in cellular oxidative stress, and its interaction with TXNDC5 in the ER may decrease the disulfide bonds of this protein. In addition, glutathione is utilized by glutathione peroxidases to inactivate oxidized lipids. To characterize proteins interacting with TXNDC5, immunoprecipitation and liquid chromatography-mass spectrometry were used. Lipid peroxidation, reduced glutathione, inducible phospholipase A2 (iPLA2) and hepatic transcriptome were assessed in the AML12 and TXNDC5-deficient AML12 cell lines. The results showed that HSPA9 and PRDX6 interact with TXNDC5 in AML12 cells. In addition, TXNDC5 deficiency reduced the protein levels of PRDX6 and HSPA9 in AML12. Moreover, lipid peroxidation, glutathione and iPLA2 activities were significantly decreased in TXNDC5-deficient cells, and to find the cause of the PRDX6 protein reduction, proteasome suppression revealed no considerable effect on it. Finally, hepatic transcripts connected to PRDX6 and HSPA9 indicated an increase in the Dnaja3, Mfn2 and Prdx5 and a decrease in Npm1, Oplah, Gstp3, Gstm6, Gstt1, Serpina1a, Serpina1b, Serpina3m, Hsp90aa1 and Rps14 mRNA levels in AML12 KO cells. In conclusion, the lipid peroxidation system and glutathione mechanism in AML12 cells may be disrupted by the absence of TXNDC5, a novel protein-protein interacting partner of PRDX6 and HSPA9.

| S-EPMC10743020 | biostudies-literature

Ribosome footprinting in the cytosol and endoplasmic reticulum

Project description:In eukaryotic cells, the spatial regulation of protein expression is frequently conferred through the coupling of mRNA localization and the local control of translation. mRNA localization to the endoplasmic reticulum (ER) is a prominent example of such regulation and serves a ubiquitous role in segregating the synthesis of secretory and integral membrane proteins to the ER. Recent genomic and biochemical studies have now expanded this view to suggest a role for the ER in global protein synthesis. We have utilized cell fractionation and ribosome profiling to obtain a genomic survey of the subcellular organization of mRNA translation and report that ribosomal loading of mRNAs, a proxy for mRNA translation, is biased to the ER. Notably, ER-associated mRNAs encoding both cytosolic and topogenic signal-encoding proteins display similar ribosome loading densities, suggesting that ER-associated ribosomes serve a global role in mRNA translation. We propose that the partitioning of mRNAs and their translation between the cytosol and ER compartments may represent a novel mechanism for the post-transcriptional regulation of gene expression. HEK293 cells were fractionated between the cytosol and endoplasmic reticulum. Within each fraction, ribosome footprints were generated and sequenced. In parallel, total mRNA was sequenced.

2011-12-20 | E-GEOD-31539 | biostudies-arrayexpress

Tunicamycin-induced Endoplasmic Reticulum-Quality Control Pathway and Endoplasmic Reticulum-Associated Degradation Mechanism in the diatom Phaeodactylum tricornutum

Project description:Tunicamycin-induced Endoplasmic Reticulum-Quality Control Pathway and Endoplasmic Reticulum-Associated Degradation Mechanism in the diatom Phaeodactylum tricornutum

| PRJNA862509 | ENA

SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis

Project description:The endoplasmic reticulum (ER) requires an oxidative environment to support the efficient maturation of secretory and membrane proteins. This is in part established by glutathione, a redox-active metabolite present in reduced (GSH) and oxidized (GSSG) forms. The ER maintains a higher GSSG:GSH ratio than the cytosol; however, the mechanisms controlling ER redox balance remain poorly understood. To address this, we developed a method for the rapid immunopurification of the ER, enabling comprehensive profiling of its proteome and metabolome. Combining this approach with CRISPR screening, we identified SLC33A1 as the major ER GSSG exporter in mammalian cells. Loss of SLC33A1 leads to GSSG accumulation in the ER and a liposome-based assay demonstrates that SLC33A1 directly transports GSSG. Cryo-EM structures and molecular dynamics simulations reveal how SLC33A1 binds GSSG and identify residues critical for its transport. Finally, an imbalance in GSSG:GSH ratio induces ER stress and dependency on the ER-associated degradation (ERAD) pathway, driven by a shift in protein disulfide isomerases (PDIs) toward their oxidized forms. Altogether, our work establishes SLC33A1-mediated GSSG export as a key mechanism for ER redox homeostasis and protein maturation.

2026-02-19 | PXD074465 | Pride

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