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G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

ABSTRACT: G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

PROVIDER: PRJNA907235 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22478180.fastq.gz	Fastqsanger.gz
	SRR22478181.fastq.gz	Fastqsanger.gz
	SRR22478182.fastq.gz	Fastqsanger.gz
	SRR22478183.fastq.gz	Fastqsanger.gz

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Similar Datasets

G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

Project description:Neurofibromatosis Type II is a genetic condition caused by loss of the NF2 gene, resulting in activation of the YAP/TAZ pathway and recurrent growth of benign tumors from Schwann cells, the glia of the peripheral nervous system. Unfortunately, no pharmacological therapy is currently available for NFII. Here, we undertake a genome-wide CRISPR/cas9 screen to search for synthetic-lethal genes that, when inhibited, cause death of NF2 mutant cells but not NF2 wildtype cells. We thereby identify ACSL3 and G6PD as two synthetic-lethal partners for NF2. We find that NF2 mutant Schwann cells are vulnerable to G6PD inhibition because they have low levels of ME1. G6PD and ME1 redundantly generate cytosolic NADPH needed by cells to fight oxidative stress. Lack of either one of the two is compatible with cell viability, but down-regulation of both leads to Schwann cell death. Since genetic deficiency for G6PD is tolerated in the human population, this raises the possibility that G6PD could be a pharmacological target for NFII.

2024-04-24 | GSE219136 | GEO

G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

2024-04-24 | GSE219135 | GEO

G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

Project description:G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

| PRJNA907229 | ENA

G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

Project description:G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

| PRJNA907236 | ENA

G6PD and ACSL3 are synthetic lethal partners of NF2 in Schwann cells

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

2024-04-24 | GSE219141 | GEO

Gene expression changes in HEI-193 (NF2-deficient Schwannoma) cells by Nf18001 or TEW7197 treatment.

Project description:Loss of NF2 (merlin) has been suggested as a genetic cause of neurofibromatosis type 2 and malignant peripheral nerve sheath tumor (MPNST). Previously, we demonstrated that NF2 sustained TGF- receptor 2 (TR2) expression and reduction or loss of NF2 activated non-canonical TGF- signaling, which reduced RKIP expression via TR1 kinase activity. Here, we show that a selective RKIP inducer (novel chemical, Nf18001) inhibits tumor growth and promotes schwannoma cell differentiation into mature Schwann cells under NF2-deficient conditions. In addition, Nf18001 is not cytotoxic to cells expressing NF2 and is not disturb canonical TGF- signaling. Moreover, the novel chemical induces expression of SOX10, a marker of differentiated Schwann cells, and promotes nuclear export and degradation of SOX2, a stem cell factor. Treatment with Nf18001 inhibited tumor growth in an allograft model with mouse schwannoma cells. These results strongly suggest that selective RKIP inducers could be useful for the treatment of neurofibromatosis type 2 as well as NF2-deficient MPNST. To know the global effect of Nf18001, we performed the microarray with HEI-193.

2021-10-22 | GSE186107 | GEO

Proteomic analysis of the NF2/Merlin Interactome by Proximity Biotinylation

Project description:Neurofibromatosis type 2 is an inherited neoplastic disease consisting of schwannomas, meningiomas, and ependymomas that is caused by inactivation of the tumor suppressor gene NF2. The NF2 gene product, merlin, has no intrinsic catalytic activity; its tumor suppressor function is mediated through the proteins with which it interacts. However, there is no consensus about which merlin interactions are necessary for tumor suppression. We used proximity biotinylation followed by mass spectrometry and direct binding assays to characterize the proteins that associate with merlin and merlin mutants in immortalized Schwann cells. We identified 52 proteins that associate with merlin, including a previously unreported merlin binding protein, ASPP2. Our results identify merlin as a component of mechanosensing signal transduction pathways in cell junctions, in the context of a specific set of structures and molecules through which it acts, in a cell type relevant to schwannoma formation.

2019-04-25 | PXD012017 | Pride

Site-specifically acetylated G6PD

Project description:Site-specifically acetylated G6PD expressed in bacteria or cultured mammalian cells by genetically encoding the incorporation of acetylated lysine. Purified G6PD (expressed in E. coli) or immunopurified G6PD (expressed in HEK293T cells) were subjected to LC-MS/MS analysis.

2023-10-24 | PXD044906 | Pride

G6PD K403 acetylation-dependent PTM

Project description:To identify acetylation-dependent posttranslational modifications (PTMs) of G6PD, site-specifically acetylated and Flag-tagged G6PD was expressed in HEK293T cells by genetically encoding the incorporation of acetylated lysine in response to an in-frame TAG stop codon. K403-acetylated G6PD (sample) and K414-acetylated G6PD (control) were co-expressed with WT Fyn kinase and a catalytically inactive mutant of Fyn (FynDN). G6PD was immunoprecipitated using anti-Flag beads before MS analysis.

2023-10-24 | PXD041775 | Pride

Transcriptomic analysis of human coronary artery endothelial cells stimulated with TNF-alpha in the presence and absence of ACSL3 siRNA

Project description:TNF-alpha has a number of pro-atherogenic effects in macrovascular endothelial cells, including induction of leukocyte adhesion molecules and chemokines. We investigated the role of acyl-CoA synthetase 3 (ACSL3) in the response of cultured human macrovascular endothelial cells to TNF-alpha. TNF-alpha induced ACSL3 both in human umbilical vein endothelial cells (HUVECs) and in human coronary artery endothelial cells (HCAECs). RNA sequencing demonstrated that knockdown of ACSL3 had no marked effects on the TNF-alpha transcriptome in HCAECs. Instead, ACSL3 was required for TNF-alpha-induced lipid droplet formation from fatty acids.

2019-11-23 | GSE134489 | GEO

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