Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

CD95/Fas ligand mRNA is toxic to cells through more than one mechanism [DISE-46]

ABSTRACT: Analysis of RISC bound short (s)RNAs in a HCT116 wild-type, Drosha k.o., and Dicer k.o. cells expressing pLenti-CD95L NP or pLenti empty vector.

ORGANISM(S): Homo sapiens

PROVIDER: GSE219222 | GEO | 2023/01/17

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

CD95/Fas ligand mRNA is toxic to cells through more than one mechanism [DISE-63]

Project description:Analysis of RISC bound short (s)RNAs in a HCT116 wild-type, Drosha k.o., and Ago 1/2/3 k.o. cells expressing pLenti-CD95L NP or pLenti empty vector.

2023-01-17 | GSE219224 | GEO

CD95/Fas ligand mRNA is toxic to cells through more than one mechanism [DISE-64]

Project description:Analysis of RISC bound short (s)RNAs in a HCT116 Drosha CD95 d.k.o. cell line expressing pLenti-CD95L and various CD95L mutant constructs.

2023-01-17 | GSE219225 | GEO

CD95/Fas ligand mRNA is toxic to cells through more than one mechanism [DISE-47]

Project description:Analysis of RISC bound short (s)RNAs in a HCT116 Drosha CD95 d.k.o. cell line expressing pLenti-CD95L and various CD95L mutant constructs.

2023-01-17 | GSE219223 | GEO

CD95/Fas ligand mRNA is toxic to cells through more than one mechanism

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

2023-01-17 | GSE219226 | GEO

CD95/Fas ligand mRNA is toxic to cells.

Project description:CD95/Fas ligand binds to the death receptor CD95 to induce apoptosis in sensitive cells. We previously reported that CD95L mRNA is enriched in sequences that, when converted to si/shRNAs, kill all cancer cells by targeting critical survival genes (Putzbach et al., 2017). We now report expression of full-length CD95L mRNA itself is highly toxic to cells and induces a similar form of cell death. We demonstrate that small (s)RNAs derived from CD95L are loaded into the RNA induced silencing complex (RISC) which is required for the toxicity and processing of CD95L mRNA into sRNAs is independent of both Dicer and Drosha. We provide evidence that in addition to the CD95L transgene a number of endogenous protein coding genes involved in regulating protein translation, particularly under low miRNA conditions, can be processed to sRNAs and loaded into the RISC suggesting a new level of cell fate regulation involving RNAi.

| S-EPMC6191286 | biostudies-literature

CD95/Fas ligand mRNA is toxic to cells

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

2018-09-20 | GSE103631 | GEO

Metalloprotease-mediated cleavage of CD95 Ligand: QTOF Xevo XS data

Project description:CD95 is a member of the TNF receptor superfamily that is ubiquitously expressed in healthy and pathological tissues. Stimulation of CD95 by its physiological ligand CD95L induces its oligomerization leading in turn to the transduction of either apoptotic or non-apoptotic signals. CD95L can exist as both membrane-anchored and soluble forms (sCD95L), the latter resulting from the proteolytic cleavage of the former. Candidate proteases able to achieve CD95L cleavage were identified as matrix metalloproteases (MMP) due to their demonstrated ability to cleave other TNF superfamily ligands. The main goal of this study was to systematically identify the MMP family members capable of cleaving CD95L and subsequently determine the corresponding cleavage sites. By using different orthogonal biochemical approaches and combining them with molecular modeling, we confirmed data from the literature regarding CD95L cleavage by MMP-3 and MMP-7. Moreover, we found that MMP-2 and MMP-12 can cleave CD95L and characterized their resulting cleavage sites. This study provides a systematic approach to analyze the cleavage of CD95L, which until now had only been poorly described.

2023-02-20 | PXD039211 | Pride

CD95/Fas increases stemness in cancer cells by inducing a STAT1 dependent Type I interferon response [array]

Project description:CD95 was found to be important for both the formation of CSCs and their maintenance. Using a stable isotope labeling by amino acids in cell culture (SILAC) analysis we have now identified STAT1 as a critical gene that mediates the CSC-driving activity of CD95. We report that chronic stimulation of CD95 by either agonist antibodies, soluble CD95L or stably expressed membrane CD95L causes both serine and tyrosine phosphorylation of STAT1 and activation of STAT1 regulated genes. The genes most significantly induced were part of an interferon (IFN)-related DNA damage resistance signature (IRDS) recently identified in a radiation resistant squamous cell carcinoma cell line Nu61 when compared to parental SCC61 cells. The IRDS was found to strongly correlate with therapy resistance (chemotherapy and radiation) in multiple cancer cells as well as in 5 human primary cancers. We now report that CD95 stimulation of breast cancer cell lines or the SCC61 cells induces the upregulation of Type I IFNs that bind to both Type I receptors IFNAR1 and IFNR2 resulting in activation of JAK kinases, activation of STAT1 and induction of a number of STAT1-regulated genes. This process can be inhibited by active caspases. Consequently, we identified Type I IFNs as drivers of cancer stemness. Knockdown of STAT1 using either siRNAs or shRNAs, or deleting two independent sites in the STAT1 gene in MCF-7 cells using the CRIPSR/Cas9 gene editing system resulted in a loss of the ability of CD95 to increase stemness. This identifies STAT1 as a critical mediator of the CSCs-inducing activity of CD95.

2017-02-16 | GSE81853 | GEO

CD95/Fas ligand mRNA is toxic to cells

Project description:CD95/Fas ligand mRNA is toxic to cells

| PRJNA403815 | ENA

CD95/Fas suppresses NF-B activation through recruitment of KPC2 in a CD95L/FasL-independent mechanism

Project description:CD95 expression is preserved in triple-negative breast cancers (TNBCs) and CD95 loss in these cells triggers the induction of a pro-inflammatory program promoting the recruitment of cytotoxic NK cells impairing tumor growth. Herein, we identify a novel interaction partner of CD95, Kip1 ubiquitination-promoting complex protein 2 (KPC2) using an unbiased proteomic approach. Independently of CD95L, CD95/KPC2 interaction contributes to the partial degradation of p105 (NFκB1) and the subsequent generation of p50 homodimers, which transcriptionally represses NF-κB-driven gene expression. Mechanistically, KPC2 interacts with the C-terminal region of CD95 and serves as an adaptor to recruit RelA (p65) and KPC1, which acts as E3 ubiquitin-protein ligase promoting the degradation of p105 into p50. Loss of CD95 in TNBC cells releases KPC2, limiting the formation of the NF-κB inhibitory homodimer complex (p50/p50), promoting NF-κB activation and the production of pro-inflammatory cytokines, that could account for the immune landscape remodeling in TNBC cells

2021-12-06 | PXD027196 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data