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LGP2 virus sensor enhances apoptosis by upregulating apoptosis-regulatory genes through TRBP-bound miRNAs during viral infection

ABSTRACT: To reveal the fuction of cytoplasmic virus sensor protein, LGP2, on RNA silencing, we analyzed gene expression profiles on HeLa WT and LGP2 knockout cells during SeV infection, which were generated with CRISPR/Cas system.

ORGANISM(S): Homo sapiens

PROVIDER: GSE135547 | GEO | 2019/11/20

REPOSITORIES: GEO

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LGP2 virus sensor regulates gene expression network mediated by TRBP-bound microRNAs.

Project description:To reveal the fuction of cytoplasmic virus sensor protein, LGP2, on RNA silencing, we analyzed gene expression profiles on HeLa WT and LGP2 knockout cells, which were generated with CRISPR/Cas system.

2018-06-29 | GSE113028 | GEO

LGP2 virus sensor enhances apoptosis by upregulating apoptosis regulatory genes through TRBP-bound miRNAs during viral infection.

Project description: Not available

| S-EPMC7026649 | biostudies-literature

LGP2 virus sensor enhances apoptosis by upregulating apoptosis-regulatory genes through TRBP-bound miRNAs during viral infection

Project description:LGP2 virus sensor enhances apoptosis by upregulating apoptosis-regulatory genes through TRBP-bound miRNAs during viral infection

| PRJNA559265 | ENA

LGP2 virus sensor regulates gene expression network mediated by TRBP-bound microRNAs.

Project description: Not available

| S-EPMC6158488 | biostudies-literature

LGP2 virus sensor regulates gene expression network mediated by TRBP-bound microRNAs.

Project description:LGP2 virus sensor regulates gene expression network mediated by TRBP-bound microRNAs.

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mRNA expression profile in LGP2 and LGP2-4KR transgenic (Tg) HEK293 cells stimulated with short poly I:C

Project description:mRNA expression profiles were compared between wild-type LGP2 and four amino acid replacement LGP2 (LGP2-4KR) cells in the presence or absence of a RIG-I ligand, short poly I:C.

2022-06-07 | GSE176363 | GEO

Caspase-mediated processing of TRBP regulates apoptosis during viral infection

Project description:RNA silencing is a post-transcriptional gene-silencing mechanism mediated by microRNAs (miRNAs). However, the regulatory mechanism of RNA silencing during viral infection is unclear. TAR RNA-binding protein (TRBP) is an enhancer of RNA silencing that induces miRNA maturation by interacting with the ribonuclease Dicer. TRBP interacts with a virus sensor protein, laboratory of genetics and physiology 2 (LGP2), in the early stage of viral infection of human cells. Next, it induces apoptosis by inhibiting the maturation of miRNAs, thereby upregulating the expression of apoptosis regulatory genes. In this study, we show that TRBP undergoes a functional conversion in the late stage of viral infection. Viral infection resulted in the activation of caspases that proteolytically processed TRBP into two fragments. The N-terminal fragment did not interact with Dicer but interacted with type I interferon (IFN) signaling modulators, such as protein kinase R (PKR) and LGP2, and induced ER stress. The end results were irreversible apoptosis and suppression of IFN signaling. Our results demonstrate that the processing of TRBP enhances apoptosis, reducing IFN signaling during viral infection.

2024-04-19 | GSE234549 | GEO

Caspase-mediated processing of TRBP regulates apoptosis during viral infection

2024-04-19 | GSE234547 | GEO

Virus Sensor RIG-I Represses RNA Interference by Interacting with TRBP through LGP2 in Mammalian Cells.

Project description: Not available

| S-EPMC6210652 | biostudies-literature

LGP2 binds PACT to regulate RIG-I- and MDA5-mediated antiviral response

Project description:The RIG-I-like receptors (RLRs: RIG-I, MDA5 and LGP2) trigger inflammatory and antiviral responses by sensing non-self RNA molecules produced during viral replication. LGP2 regulation of RIG-I and MDA5-dependant type-I interferon signaling is a matter of controversy. Here we show that LGP2 interacts with different components of the RNA silencing machinery. Particularly, we identified a direct protein-protein interaction between LGP2 and interferon-inducible double-stranded RNA-dependent protein kinase activator A (PACT). The LGP2-PACT interaction is mediated by the regulatory C-terminal domain of LGP2 and is necessary for inhibiting the RIG-I- and amplifying the MDA5-responses. We describe a point mutation within LGP2 that disrupts LGP2-PACT interaction and leads to the loss of LGP2 regulatory activity over RIG-I and MDA5. These results provide a model in which PACT-LGP2 interaction regulates RIG-I and MDA5 inflammatory response and allows cellular RNA silencing machinery to coordinate the innate immune response.

2019-10-02 | PXD013191 | Pride

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