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

ABSTRACT: 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.

ORGANISM(S): Homo sapiens

PROVIDER: GSE219225 | GEO | 2023/01/17

REPOSITORIES: GEO

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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.

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

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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

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

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