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Caspase-mediated processing of TRBP regulates apoptosis during viral infection

ABSTRACT: Caspase-mediated processing of TRBP regulates apoptosis during viral infection

PROVIDER: PRJNA982025 | ENA |

REPOSITORIES: ENA

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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

Caspase-mediated processing of TRBP regulates apoptosis during viral infection

Project description:Caspase-mediated processing of TRBP regulates apoptosis during viral infection

| PRJNA982032 | ENA

Caspase-mediated processing of TRBP regulates apoptosis during viral infection

Project description:Caspase-mediated processing of TRBP regulates apoptosis during viral infection

| PRJNA982029 | ENA

Caspase-mediated processing of TRBP regulates apoptosis during viral infection

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

2024-04-19 | GSE234550 | GEO

Homo sapiens strain:HeLa

Project description:Caspase-mediated processing of TRBP regulates apoptosis during viral infection

| PRJDB17739 | ENA

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

Deletion of human tarbp2 reveals cellular microRNA targets and cell cycle function of TRBP

Project description:TRBP has two known functions as Dicer co-factor and PKR inhibitor. However, the role of TRBP in miRNA biogenesis is controversial and its regulation of PKR in mitosis remains unexplored. Here, we generate TRBP KO HeLa cells and find that TRBP depletion alters Dicer processing sites of a subset of miRNAs, but does not affect Dicer stability, miRNA abundance, or Argonaute loading. By generating PACT, another Dicer interactor, and TRBP/PACT double-KO cells, we further show that TRBP and PACT do not functionally compensate each other and that only TRBP contributes to Dicer processing. We also report that TRBP is hyperphosphorylated by JNK in M phase when PKR is activated by cellular dsRNAs. Hyperphosphorylation potentiates the inhibitory activity of TRBP on PKR, suppressing PKR in M-G1 transition. By generating the first human TRBP KO, our study clarifies the role of TRBP and unveils negative feedback regulation of PKR through TRBP phosphorylation.

2014-09-16 | GSE61458 | GEO

Deletion of human tarbp2 reveals cellular microRNA targets and cell cycle function of TRBP

2014-09-16 | E-GEOD-61458 | biostudies-arrayexpress

NS7a of SADS-CoV promotes viral infection via inducing apoptosis to suppress Type III interferon production

Project description:SADS-CoV is a newly discovered swine coronavirus with potential cross-species transmission risk. Although SADS-CoV-induced host cell apoptosis and attenuated innate immunity has been established, the relation between apoptosis and innate immunity remain obscure. Here, we demonstrate that infection of SADS-CoV induced apoptosis in vivo and in vitro, and that viral protein NS7a is mainly responsible for SADS-CoV-induced apoptosis in host cells. Furthermore, we found that NS7a interacted with apoptosis inducing factor mitochondria associated 1 (AIFM1) to activate caspase-3 via caspase-6 in SADS-CoV-infected cells, and enhanced SADS-CoV replication. Importantly, NS7a suppressed Poly(I:C)-induced expression of Type III interferon (IFN-λ) via activation caspase-3 to cleave IRF3, and caspase-3 inhibitor protects piglets against SADS-CoV infection in vivo. These findings reveal how SADS-CoV-induced apoptosis to inhibit innate immunity and provide a valuable clue to the development of effective drugs for the clinical control of SADS-CoV infection.

2025-05-06 | PXD047032 | Pride

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