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

ABSTRACT: 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.

ORGANISM(S): Mus musculus

PROVIDER: GSE318827 | GEO | 2026/02/12

REPOSITORIES: GEO

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SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis

Project description:Endoplasmic reticulum (ER) fractions were purified from HEK293T cells expressing ER-tag or control-tag constructs and analyzed by quantitative proteomics to assess enrichment of ER proteins and define ER proteome composition. Proteomic analysis demonstrated selective enrichment of annotated ER proteins relative to other cellular compartments. A curated reference set of ER-associated proteins was used to benchmark coverage. Approximately 800 proteins were significantly enriched over control immunoprecipitations, of which 508 matched curated ER-associated proteins.

2026-02-13 | PXD074236 | Pride

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

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

Project description:Tunicamycin inhibits the first step of protein N-glycosylation modification. However, the physiological, transcriptomic, and N-glycomic effects of tunicamycin on important marine diatom Phaeodactylum tricornutum are still unknown. In this study, comprehensive approaches were used to study the effects. The results showed that cell growth and photosynthesis were significantly inhibited in P. tricornutum under the tunicamycin stress. The soluble protein content was significantly decreased, while the soluble sugar and neutral lipid were dramatically increased to orchestrate the balance of carbon and nitrogen metabolism. 0.3 μg m-1 tunicamycin could not complete inhibited the N-glycosylation of protein, but it resulted in the differentially expression of ERQC and ERAD related genes. The upregulation of genes involved in ERQC and the activation of anti-oxidases were speculated to alleviate the tunicamycin stress. The differentially expression of genes related to ERAD was suggested to degrade the unfolded and/or incorrect N-glycoproteins induced by tunicamycin. The identification of mannose-type and complex-type N-glycan structures enriched the N-glycan database of diatom P. tricornutum and provided important information for studying the function of N-glycosylation modification on proteins. All in all, the proposed working models of ERQC and ERAD will provide a solid foundation for further in-depth study the related mechanism and the diatom expression system.

2022-08-02 | GSE209809 | GEO

Nuclear receptor LRH-1/NR5A2 is required and targetable for liver endoplasmic reticulum stress resolution.

Project description:Chronic endoplasmic reticulum (ER) stress results in toxicity that contributes to multiple human disorders. We report a stress resolution pathway initiated by the nuclear receptor LRH-1 that is independent of known unfolded protein response (UPR) pathways. Like mice lacking primary UPR components, hepatic Lrh-1-null mice cannot resolve ER stress, despite a functional UPR. In response to ER stress, LRH-1 induces expression of the kinase Plk3, which phosphorylates and activates the transcription factor ATF2. Plk3-null mice also cannot resolve ER stress, and restoring Plk3 expression in Lrh-1-null cells rescues ER stress resolution. Reduced or heightened ATF2 activity also sensitizes or desensitizes cells to ER stress, respectively. LRH-1 agonist treatment increases ER stress resistance and decreases cell death. We conclude that LRH-1 initiates a novel pathway of ER stress resolution that is independent of the UPR, yet equivalently required. Targeting LRH-1 may be beneficial in human disorders associated with chronic ER stress. 24 total samples. One sample represents one mouse. Three samples were analyzed from the following groups: Lrh-1 f/f (control littermates) treated with vehicle, Lrh-1 f/f treated with tunicamycin (TM; 1mg/kg BW for 24h), Lrh-1 f/f treated with tunicamycin and DLPC (100mg/kg BW 4x), Lrh-1 f/f treated with tunicamycin and vehicle for DLPC, Lrh-1 liver-specific KO mice (LKO) treated with vehicle, Lrh-1 LKO treated with tunicamycin, and Lrh-1 LKO treated with tunicamycin and DLPC, Lrh-1 LKO treated with tunicamycin and vehicle for DLPC

2015-05-12 | E-GEOD-68718 | biostudies-arrayexpress

GENE EXPRESSION ANALYSIS IN TOMATO (Lycopersicon esculentum) UNDER ENDOPLASMIC RETICULUM (ER) STRESS

Project description:To investigate the effect of ER stress on gene expressions in Tomato, RNA-seq was performed on 2 hours and 6 hours of tunicamycin applied samples.

2024-12-24 | GSE220689 | GEO

NADPH and Glutathione Redox Link TCA Cycle Activity to Endoplasmic Reticulum Homeostasis.

Project description:Many metabolic diseases disrupt endoplasmic reticulum (ER) homeostasis, but little is known about how metabolic activity is communicated to the ER. Here, we show in hepatocytes and other metabolically active cells that decreasing the availability of substrate for the tricarboxylic acid (TCA) cycle diminished NADPH production, elevated glutathione oxidation, led to altered oxidative maturation of ER client proteins, and attenuated ER stress. This attenuation was prevented when glutathione oxidation was disfavored. ER stress was also alleviated by inhibiting either TCA-dependent NADPH production or Glutathione Reductase. Conversely, stimulating TCA activity increased NADPH production, glutathione reduction, and ER stress. Validating these findings, deletion of the Mitochondrial Pyruvate Carrier-which is known to decrease TCA cycle activity and protect the liver from steatohepatitis-also diminished NADPH, elevated glutathione oxidation, and alleviated ER stress. Together, our results demonstrate a novel pathway by which mitochondrial metabolic activity is communicated to the ER through the relay of redox metabolites.

| S-EPMC7254477 | biostudies-literature

Sse1, Hsp110 chaperone of yeast, controls the cellular fate during Endoplasmic Reticulum-stress

Project description:Sse1, yeast cytosolic Hsp110 chaperone, is a wellknown Nucleotide Exchange Factor (NEF), a protein-disaggregase and a Chaperone linked to Protein Synthesis (CLIPS). Here we demonstrate SSE1’s genetic interaction with IRE1 and HAC1, the Endoplasmic Reticulum-Unfolded Protein Response (ER-UPR) sensors. sse1Δ strain exhibits an ER-UPR signalling-dependent resistance to tunicamycin-induced ER stress. Importantly, ER-stress-responsive reorganization of translating ribosomes from polysomes to monosomes is inefficient in SSE1 deleted strain leading to uninterrupted protein translation and starkly different ER-UPR kinetics. sse1Δ exhibits faster ER-UPR induction and quicker reversal to basal state compared to wildtype (WT) cells. Interestingly, ER-stress mediated yeast cell division arrest is escaped in sse1Δ strain during long term tunicamycin stress indicating important role of this chaperone in controlling cell division during ER stress. Furthermore, sse1Δ strain shows significantly higher cell viability in comparison to WT yeast, following short-term as well as long-term tunicamycin stress. In summary, we show that cytosolic chaperone Sse1 genetically interacts with ER-UPR pathway, controls the kinetics of ER-UPR, stress-induced cell division arrest and cell viability during global ER stress by tunicamycin.

2024-04-19 | PXD045382 | Pride

SILAC-based quantitative proteomics of endoplasmic reticulum stress

Project description:ER stress and the unfolded protein response (UPR) involve extensive proteome remodeling in many cell compartments. However, a comprehensive analysis has been lagging due to technological limitations. Here we employ SILAC-based proteomics to quantify over 6,200 proteins at increasing concentrations of tunicamycin in HeLa cells. We further compare the effects of tunicamycin to those of thapsigargin and DTT, both activating the UPR through different mechanisms. The systematic description of the proteome-wide expression changes following proteostatic stress is a resource for the scientific community, which enables to discover novel players involved the pathophysiology of disorders linked to proteostasis. Here, we identified 38 proteins, not previously linked to the UPR, whose expression increases, of which 15 would likely remediate ER stress, and the remainder may contribute to pathological outcomes. Unexpectedly, we see few strongly downregulated proteins, despite expression of the pro-apoptotic transcription factor CHOP, suggesting that IRE1-dependent mRNA decay (RIDD) has a limited contribution to ER-stress mediated cell death in our system.

2019-11-01 | PXD013496 | Pride

Endoplasmic reticulum (ER) stress and the unfolded protein response (UPR)

Project description:We are currently studying how these information-carrying oligosaccharides are involved in cellular stress responses, particularly in human genetic diseases called Congenital Disorders Of Glycosylation in which oligosaccharide assembly is defective. We are interested in endoplasmic stress responses/unfolded protein responses. ER glycans and ER lectins are intimately involved in the folding of ER proteins. Therefore, ER lectins and ER glycosyltransferases may be controlled by these stress responses, to produce and/or recognize key glycans in the stress response. Our model system is the human dermal fibroblast. We have successfully calibrated the ER stress responses in these cells by determining the magnitudes of various stress effects (such as chaperone transcription) with different forms of ER stress. We are also completing a study in which activation the signaling molecules Ire1 and ATF6 are also calibrated. We prepared multiple identical aliquots of RNA from cells stressed under several of these calibrated conditions. Endoplasmic reticulum (ER) stress and the unfolded protein response (UPR): Study of the role of ER stress in the expression of genes for ER transferases and lectins that participate in ER folding and quality control using human skin fibroblasts. The UPR response in these cells has been calibrated using various readouts in response to different stresses: 1) 40 nM L-azetidine-2-carboxylate (AZC) 1 hour, 2) 0.2 mg/ml castanospermine, 24 hours, 3) 2 mM Dithiothreitol (DTT), 20 minutes, 4) 100nm Thapsigargin (TG), 30 minutes, 5) 5 ug/ml tunicamycin, 5 hours, 6) untreated control cells

2011-02-17 | E-GEOD-27349 | biostudies-arrayexpress

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