Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly
Mohamed Emara,Margo A. Brinton +1 more
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The interaction of TIAR with viral components facilitates flavivirus genome RNA synthesis and inhibits SG formation, which prevents the shutoff of host translation.Abstract:
The West Nile virus minus-strand 3' terminal stem loop (SL) RNA was previously shown to bind specifically to cellular stress granule (SG) components, T cell intracellular antigen-1 (TIA-1) and the related protein TIAR. In vitro TIAR binding was 10 times more efficient than TIA-1. The 3'(-)SL functions as the promoter for genomic RNA synthesis. Colocalization of TIAR and TIA-1 with the viral replication complex components dsRNA and NS3 was observed in the perinuclear regions of West Nile virus- and dengue virus-infected cells. The kinetics of accumulation of TIAR in the perinuclear region was similar to those of genomic RNA synthesis. In contrast, relocation of TIA-1 to the perinuclear region began only after maximal levels of RNA synthesis had been achieved, except when TIAR was absent. Virus infection did not induce SGs and progressive resistance to SG induction by arsenite developed coincident with TIAR relocation. A progressive decrease in the number of processing bodies was secondarily observed in infected cells. These data suggest that the interaction of TIAR with viral components facilitates flavivirus genome RNA synthesis and inhibits SG formation, which prevents the shutoff of host translation.read more
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Stress granules: the Tao of RNA triage
Paul A. Anderson,Nancy Kedersha +1 more
TL;DR: Although both self-assemble in response to stress-induced perturbations in translation, several recent reports reveal novel proteins and RNAs that are components of these structures but also perform other cellular functions.
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RNA interference screen for human genes associated with West Nile virus infection.
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Inhibition of Cytoplasmic mRNA Stress Granule Formation by a Viral Proteinase
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References
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Flaviviridae :T he Viruses and Their Replication
TL;DR: The present research attacked the Flavivirus infection through two mechanisms: Membrane Reorganization and the Compartmentalization and Assembly and Release of Particles from Flaviv virus-infected Cells and Host Resistance to Flaviviral Infection.
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Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
Nancy Kedersha,Georg Stoecklin,Maranatha Ayodele,Patrick W. Yacono,Jens Lykke-Andersen,Marvin J. Fritzler,Donalyn Scheuner,Randal J. Kaufman,David E. Golan,Paul A. Anderson +9 more
TL;DR: It is proposed that mRNA released from disassembled polysomes is sorted and remodeled at SGs, from which selected transcripts are delivered to PBs for degradation, an interaction that is promoted by the related mRNA decay factors TTP and BRF1.
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RNA-Binding Proteins Tia-1 and Tiar Link the Phosphorylation of Eif-2α to the Assembly of Mammalian Stress Granules
TL;DR: The ability of a TIA-1 mutant lacking its RNA-binding domains to function as a transdominant inhibitor of SG formation suggests that this RNA- binding protein acts downstream of the phosphorylation of eIF-2α to promote the sequestration of untranslated mRNAs at SGs.
Journal ArticleDOI
P bodies: at the crossroads of post-transcriptional pathways
TL;DR: The available evidence indicates that P bodies are sites where mRNAs that are not being translated accumulate, the information carried by associated proteins and regulatory RNAs is integrated, and their fate — either translation, silencing or decay — is decided.
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Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1
Natalie Gilks,Nancy Kedersha,Maranatha Ayodele,Lily Shen,Georg Stoecklin,Laura M. Dember,Laura M. Dember,Paul A. Anderson +7 more
TL;DR: Prion-like aggregation of TIA-1 regulates SG formation downstream of eIF2alpha phosphorylation in response to stress, confirming that a prion domain can mediate the assembly of SGs.