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Persistent ER stress in maize seedlings engages ZmIRE1 in a multiphasic process that transitions from prosurvival activities to cell death [RNA-Seq]

ABSTRACT: We tracked the gene expression events following treatment of maize seedlings with the endoplasmic reticulum (ER) stress agent tunicamycin. ER stress elicits the unfolded protein response (UPR) and when plants are faced with persistent stress, the UPR transitions from an adaptive or cell survival phase to programmed cell death.

ORGANISM(S): Zea mays

PROVIDER: GSE111250 | GEO | 2018/05/30

REPOSITORIES: GEO

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Persistent ER stress in maize seedlings engages ZmIRE1 in a multiphasic process that transitions from prosurvival activities to cell death [ATAC-Seq]

Project description:Nucleus was isolated from flash frozen from tunicamycin treated (0,6 and 12 hours) maize root samples, purified, then transposition reaction and and purification steps were carried out following the standard ATAC-seq protocol

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

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

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

Ribosomal protein S7 ubiquitination during ER stress in yeast is associated with selective mRNA translation and stress outcome.

Project description:eIF2α phosphorylation-mediated translational regulation is crucial for global translation repression by various stresses, including the unfolded protein response (UPR). However, translational control during UPR has not been demonstrated in yeast. This study investigated ribosome ubiquitination-mediated translational controls during UPR. Tunicamycin-induced ER stress enhanced the levels of ubiquitination of the ribosomal proteins uS10, uS3 and eS7. Not4-mediated monoubiquitination of eS7A was required for resistance to tunicamycin, whereas E3 ligase Hel2-mediated ubiquitination of uS10 was not. Ribosome profiling showed that the monoubiquitination of eS7A was crucial for translational regulation, including the upregulation of the spliced form of HAC1 (HAC1i) mRNA and the downregulation of Histidine triad NucleoTide-binding 1 (HNT1) mRNA. Downregulation of the deubiquitinating enzyme complex Upb3-Bre5 increased the levels of ubiquitinated eS7A during UPR in an Ire1-independent manner. These findings suggest that the monoubiquitination of ribosomal protein eS7A plays a crucial role in translational controls during the ER stress response in yeast.

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SILAC-based quantitative proteomics of endoplasmic reticulum stress

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2019-11-01 | PXD013496 | Pride

Persistent ER stress in maize seedlings engages ZmIRE1 in a multiphasic process that transitions from prosurvival activities to cell death

Project description:This SuperSeries is composed of the SubSeries listed below.

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Effect of Tunicamycin on Bovine Capillary Endothelial Cells

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Transcriptome profile of S. cerevisiae treated with tauroursodeoxycholic acid (TUDCA)

Project description:Cells respond to endoplasmic reticulum (ER) stress through activation of signaling pathways such as the Unfolded Protein Response (UPR) which improve the ER folding environment capacity upon changes in misfolded protein burden. Small molecules termed chemical chaperones can attenuate the UPR under stress conditions and improve folding and trafficking of specific mutant proteins. One such compound is the bile acid tauroursodeoxycholic acid (TUDCA). Despite promising results in multiple models of protein folding diseases, TUDCA’s mechanism of action remains unclear. To better define how TUDCA attenuate ER stress, we leveraged the genetically tractable budding yeast, S. cerevisiae. Consistent with properties described for TUDCA, we found it significantly improves growth of yeast subjected to ER stress caused by the N-glycosylation inhibitor tunicamycin (Tm) independently of activity of the UPR. In addition to other data, transcriptomics of strains treated with TUDCA link its ability to resuce Tm-induced stress with cell wall remodeling.

2024-11-13 | GSE186390 | GEO

Secretome characterization of nucleus pulposus (NP) cells subjected to ER stress

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2020-12-03 | PXD019151 | Pride

RNA-seq of WT vs isw1 delta S. cerevisiae cells during Unfolded Protein Response time course

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2022-10-06 | E-MTAB-10511 | biostudies-arrayexpress

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