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Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer

ABSTRACT: Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer

PROVIDER: PRJNA946144 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23891442_1.fastq.gz	Fastqsanger.gz
	SRR23891442_2.fastq.gz	Fastqsanger.gz
	SRR23891443_1.fastq.gz	Fastqsanger.gz
	SRR23891443_2.fastq.gz	Fastqsanger.gz
	SRR23891444_1.fastq.gz	Fastqsanger.gz

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Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer [RNA-seq II]

Project description:To investigate if oxaliplatin resistance contributed to persistent endoplasmic reticulum-induced senescence,

2023-03-22 | GSE227609 | GEO

Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer [RNA-seq II]

Project description:Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer [RNA-seq II]

| PRJNA945902 | ENA

Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer [RNA-seq I]

Project description:Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer [RNA-seq I]

| PRJNA944924 | ENA

Inositol triphosphate-triggered calcium release blocks lipid exchange at endoplasmic reticulum-Golgi contact sites

Project description:Vesicular traffic and membrane contact sites between organelles enable the exchange of proteins, lipids, and metabolites. Recruitment of membrane tethers to contact sites between the endoplasmic reticulum (ER) and the plasma membrane is often triggered by calcium. In contrast, we reveal here a function for calcium in the repression of cholesterol export at membrane contact sites between the ER and the Golgi complex. We show that calcium efflux from ER stores induced by inositol-triphosphate [IP3] accumulation upon loss of the inositol 5-phosphatase INPP5A or sustained receptor signaling triggers the depletion of cholesterol and associated complex glycosphingolipids from the cell surface, resulting in a blockade of clathrin-independent endocytosis (CIE) of bacterial Shiga toxin. This phenotype is caused by the calcium-induced dissociation of oxysterol binding protein (OSBP) from the Golgi complex and from VAP-containing membrane contact sites. Our findings reveal a crucial function for INPP5A-mediated IP3 hydrolysis in the control of lipid exchange at membrane contact sites.

2021-05-06 | MTBLS2444 | MetaboLights

Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer

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

2023-03-22 | GSE227641 | GEO

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

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Inositol hexaphosphate enhances chemotherapy by reversing persistent endoplasmic reticulum stress-induced senescence in colorectal cancer [RNA-seq I]

Project description:To investigate if CRC cells treated with CoCl2, brefeldin A, or low glucose for more than 30 days exhibited an increased senescence.

2023-03-22 | GSE227379 | GEO

EMD37 triggers endoplasmic reticulum stress in cancer cells

Project description:EMD37 triggers endoplasmic reticulum stress in cancer cells

| PRJNA828545 | ENA

The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

Project description:In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.

2016-11-30 | GSE85686 | GEO

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