Non‐structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double‐stranded RNA‐binding protein, staufen1

Cho, Hana; Ahn, Sang Ho; Kim, Kyoung Mi; Kim, Yoon Ki

doi:10.1016/j.febslet.2013.05.029

Cited by 10 publications

(9 citation statements)

References 33 publications

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“…The common enriched pathways among ProTINA, DeMAND and DE (top of Figure 6 ) included known mechanisms related to viral entry, replication and assembly, including endocytosis ( 61 ), protein processing in endoplasmic reticulum ( 62 ), ubiquitin mediated proteolysis ( 63 , 64 ) and RIG-I-like receptor signaling pathway ( 65 , 66 ). Both ProTINA and DE analysis indicated the modulation of host cell cycle ( 67 ), mRNA surveillance ( 68 ) and DNA damage response ( 69 ). Only ProTINA prediction was significantly enriched for focal adhesion and actin cytoskeleton, which have been shown to regulate influenza virus entry at the early stage of infection ( 70 ).…”

Section: Resultsmentioning

confidence: 99%

Network perturbation analysis of gene transcriptional profiles reveals protein targets and mechanism of action of drugs and influenza A viral infection

Noh

Shoemaker

2018

Nucleic Acids Research

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Genome-wide transcriptional profiling provides a global view of cellular state and how this state changes under different treatments (e.g. drugs) or conditions (e.g. healthy and diseased). Here, we present ProTINA (Protein Target Inference by Network Analysis), a network perturbation analysis method for inferring protein targets of compounds from gene transcriptional profiles. ProTINA uses a dynamic model of the cell-type specific protein–gene transcriptional regulation to infer network perturbations from steady state and time-series differential gene expression profiles. A candidate protein target is scored based on the gene network's dysregulation, including enhancement and attenuation of transcriptional regulatory activity of the protein on its downstream genes, caused by drug treatments. For benchmark datasets from three drug treatment studies, ProTINA was able to provide highly accurate protein target predictions and to reveal the mechanism of action of compounds with high sensitivity and specificity. Further, an application of ProTINA to gene expression profiles of influenza A viral infection led to new insights of the early events in the infection.

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Section: Resultsmentioning

confidence: 99%

Network perturbation analysis of gene transcriptional profiles reveals protein targets and mechanism of action of drugs and influenza A viral infection

Noh

Shoemaker

2018

Nucleic Acids Research

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“…Since NS5B, NS5A, NS3 and HCVRNA are constituents of the HCV replication complex, the interaction of Stau1 with these constituents could as well be part of the replication complex, besides facilitating transport of HCV RNA at the site of translation or replication. Stau1 also influences the replication and infectivity of Influenza virus via its interaction with viral protein, NS1 ( 25 , 64 ). It plays an important role in HIV-1 assembly, replication, translation and generation of infectious virions particles ( 65–67 ).…”

Section: Discussionmentioning

confidence: 99%

Staufen1 promotes HCV replication by inhibiting protein kinase R and transporting viral RNA to the site of translation and replication in the cells

et al. 2016

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Persistent hepatitis C virus (HCV) infection leads to chronic hepatitis C (CHC), which often progresses to liver cirrhosis (LC) and hepatocellular carcinoma (HCC). The molecular mechanisms that establish CHC and cause its subsequent development into LC and HCC are poorly understood. We have identified a cytoplasmic double-stranded RNA binding protein, Stau1, which is crucial for HCV replication. In this study, Stau1 specifically interacted with the variable-stem-loop region in the 3′ NTR and domain IIId of the HCV-IRES in the 5′ NTR, and promoted HCV replication and translation. Stau1 coimmunoprecipitates HCV NS5B and a cell factor, protein kinase R (PKR), which is critical for interferon-induced cellular antiviral and antiproliferative responses. Like Stau1, PKR displayed binding specificity to domain IIId of HCV-IRES. Stau1 binds to PKR and strongly inhibits PKR-autophosphorylation. We demonstrated that the transport of HCV RNA on the polysomes is Stau1-dependent, being mainly localized in the monosome fractions when Stau1 is downregulated and exclusively localized in the polysomes when Stau1 is overexpressed. Our findings suggest that HCV may appropriate Stau1 to its advantage to prevent PKR-mediated inhibition of eIF2α, which is required for the synthesis of HCV proteins for translocation of viral RNA genome to the polysomes for efficient translation and replication.

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“…Microarray analysis was performed by Macrogen, as described previously (9,10,50). The microarray data were deposited in the National Center for Biotechnology Information Gene Expression Omnibus web-based data repository (series ID: GSE49591).…”

Section: Methodsmentioning

confidence: 99%

Glucocorticoid receptor interacts with PNRC2 in a ligand-dependent manner to recruit UPF1 for rapid mRNA degradation

Cho

Park

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Glucocorticoid receptor (GR), which was originally known to function as a nuclear receptor, plays a role in rapid mRNA degradation by acting as an RNA-binding protein. The mechanism by which this process occurs remains unknown. Here, we demonstrate that GR, preloaded onto the 5′UTR of a target mRNA, recruits UPF1 through proline-rich nuclear receptor coregulatory protein 2 (PNRC2) in a ligand-dependent manner, so as to elicit rapid mRNA degradation. We call this process GR-mediated mRNA decay (GMD). Although GMD, nonsense-mediated mRNA decay (NMD), and staufen-mediated mRNA decay (SMD) share upstream frameshift 1 (UPF1) and PNRC2, we find that GMD is mechanistically distinct from NMD and SMD. We also identify de novo cellular GMD substrates using microarray analysis. Intriguingly, GMD functions in the chemotaxis of human monocytes by targeting chemokine (C-C motif) ligand 2 (CCL2) mRNA. Thus, our data provide molecular evidence of a posttranscriptional role of the well-studied nuclear hormone receptor, GR, which is traditionally considered a transcription factor. glucocorticoid receptor | PNRC2 | UPF1 | glucocorticoid receptor-mediated mRNA decay | Nonsense-mediated mRNA decay A t the cellular level, glucocorticoid receptor (GR), which belongs to the nuclear receptor superfamily, functions as a transcription factor regulating various physiological processes (1-3). In the presence of a glucocorticoid, which diffuses through the plasma membrane into the cytoplasm, cytosolic GR binds to the glucocorticoid. The resulting glucocorticoid-GR complex is activated and then enters the nucleus. Once in the nucleus, GR dimerizes, binds to specific cis-acting elements, and recruits coregulatory proteins for transcriptional activation or repression (4, 5).The majority of the coregulatory proteins commonly contain a nuclear receptor box (NR box, also called an LXXLL motif), which is important for interactions between coregulatory proteins and nuclear receptors (4-6). The proline-rich nuclear receptor coregulatory protein (PNRC), however, is an exception because it interacts with nuclear receptors through an SH3-binding motif [SD(E)PPSPS] rather than an NR box (7,8). Two PNRC paralogs, PNRC1 and PNRC2, have been identified in mammalian cells (7,8). PNRC1 and PNRC2 are believed to play similar roles in nuclear receptor-mediated signaling because they interact with similar groups of nuclear receptors.Although PNRC2 is known to function as a coregulatory protein for nuclear receptors, it has a distinct function in mRNA decay pathways including nonsense-mediated mRNA decay (NMD), staufen (STAU)-mediated mRNA decay (SMD), and replication-dependent histone mRNA degradation (HMD) (9-13). NMD serves as a mechanism of both mRNA quality control and posttranscriptional regulation by selectively recognizing and degrading cellular transcripts that are abnormal or that contain a premature translation termination codon (PTC), as reviewed elsewhere (14-16). A key NMD factor, UPF1, is recruited to a terminating ribosome at a PTC. UPF1 then recr...

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Non‐structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double‐stranded RNA‐binding protein, staufen1

Cited by 10 publications

References 33 publications

Network perturbation analysis of gene transcriptional profiles reveals protein targets and mechanism of action of drugs and influenza A viral infection

Network perturbation analysis of gene transcriptional profiles reveals protein targets and mechanism of action of drugs and influenza A viral infection

Staufen1 promotes HCV replication by inhibiting protein kinase R and transporting viral RNA to the site of translation and replication in the cells

Glucocorticoid receptor interacts with PNRC2 in a ligand-dependent manner to recruit UPF1 for rapid mRNA degradation

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