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The integrated stress response protects microtubule dynamics to recover from proteotoxic stress

ABSTRACT: The integrated stress response protects microtubule dynamics to recover from proteotoxic stress

PROVIDER: PRJNA798445 | ENA |

REPOSITORIES: ENA

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The integrated stress response protects microtubule dynamics to recover from proteotoxic stress

Project description:By performing ribosome profiling on squamous cell carcinoma stem cells (either control or S51A mutant) we found that the ISR translationally regulates a network of centrosomal proteins to help cellular recovery upon proteotoxic stress.

2022-07-15 | GSE193945 | GEO

RNA-seq: WT under proteotoxic stress conditions

Project description:In order to elucidate on mRNA changes upon various proteotoxic stress conditions, synchronized WT (N2) worms were treated from L4 to day 1 of adulthood and collected for RNA extraction in the following

2019-01-01 | GSE124178 | GEO

RNA-seq: WT under proteotoxic stress conditions

Project description:RNA-seq: WT under proteotoxic stress conditions

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Proteotoxic stress-induced apoptosis in cancer cells: understanding the susceptibility and enhancing the potency

Project description:Leiomyosarcoma (LMS) is an aggressive cancer with few therapeutic options. LMS cells are more sensitive to proteotoxic stress compared to normal smooth muscle cells. We used small compound 2c to induce proteotoxic stress and compare the transcriptomic adaptations of immortalized human uterine smooth muscle cells (HUtSMC) and LMS cells SK-UT-1. We found that the expression of the heat shock proteins (HSP) gene family is upregulated with higher efficiency in normal cells. In contrast, upregulation of BH3-only proteins is higher in LMS cells. HSF1, the master regulator of HSP transcription, is sequestered into transcriptionally incompetent nuclear foci only in LMS cells, which explains the lower HSP upregulation. We also found that several compounds can enhance the cell death response to proteotoxic stress. Specifically, when low doses were used, an inhibitor of salt-inducible kinases (SIKs) and the inhibitor of IRE1, a key element of the unfolded protein response (UPR), support proteotoxic-induced cell death with strength in LMS cells and without effects on the survival of normal cells. Overall, our data provide an explanation for the higher susceptibility of LMS cells to proteotoxic stress and suggest a potential option for co-treatment strategies.

2022-10-03 | GSE205596 | GEO

Effect of peroxisomal proteotoxic stress on gene expression in mammalian cells

Project description:To establish the overall cell responses to peroxisomal proteotoxic stress, we analysed transcriptomes of NT- and LONP2-silenced cells using RNA sequencing in COS-7 and U2OS cells.

2023-09-27 | GSE224992 | GEO

The Lon protease links nucleotide metabolism with proteotoxic stress

Project description:Purpose: Next-generation sequencing (NGS) has revolutionized systems-based analysis of cellular pathways. The goals of this study are to compare NGS-derived transcriptome profiling (RNA-seq) and transposon insertion mutagenesis (Tnseq) libraries of Lon deletions compared to wt Caulobacter crescentus. Methods: See Methods section of The Lon protease links nucleotide metabolism with proteotoxic stress for information regarding methods or contact lead correspondence. Briefly, Samples for RNAseq were extracted from wt and lon deletion strains grown to mid exponential phase. Methods: See Methods section of The Lon protease links nucleotide metabolism with proteotoxic stress for information regarding methods or contact lead correspondence. Briefly, Samples for Tnseq were generated by Eztn5 transposon mutagenesis. Conclusions: Our study represents the first detailed analysis of lon deletion comparison to wt caulobacter transcriptomes, with biologic replicates, generated by RNA-seq technology.

2020-06-14 | GSE152426 | GEO

The Lon protease links nucleotide metabolism with proteotoxic stress

Project description:The Lon protease links nucleotide metabolism with proteotoxic stress

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HRD1-mediated METTL14 degradation regulates m6A mRNA modification to suppress ER proteotoxic liver disease

Project description:Accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) lumen triggers unfolded protein response (UPR) for stress adaptation, the failure of which induces cell apoptosis and tissue/organ damage. The molecular switches underlying how the UPR selects for stress adaptation over apoptosis remain unknown. Here we discovered that accumulation of unfolded/misfolded proteins selectively induces N6-adenosine-methyltransferase-14 (METTL14) expression. METTL14 promotes CHOP mRNA decay through its 3’UTR N6-adenosine methylation (m6A) to inhibit its downstream pro-apoptotic target genes expression. UPR induces METTL14 expression through competing the HRD1-ERAD machinery to block METTL14 ubiquitination and degradation. Therefore, mice with liver-specific METTL14 deletion are highly susceptible to both acute pharmacological and alpha-1 antitrypsin (AAT) deficiency-induced ER proteotoxic stress and liver injury. Further hepatic CHOP deletion protects METTL14 knockout mice from ER stress-induced liver damage. Our study reveals a crosstalk between ER stress and mRNA m6A pathways, the ERm6A pathway, for ER stress adaptation to proteotoxicity.

2021-09-30 | GSE185109 | GEO

Aneuploidy-induced proteotoxic stress can be effectively tolerated without dosage compensation, genetic mutations or stress responses

Project description:Aneuploidy-induced proteotoxic stress can be effectively tolerated without dosage compensation, genetic mutations or stress responses

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Advanced genomics identifies growth effectors for proteotoxic ER stress recovery in Arabidopsis thaliana

Project description:Advanced genomics identifies growth effectors for proteotoxic ER stress recovery in Arabidopsis thaliana

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