P Bodies, Stress Granules, and Viral Life Cycles

Beckham, Carla; Parker, Roy

doi:10.1016/j.chom.2008.03.004

Cited by 205 publications

(224 citation statements)

References 69 publications

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“…Most strikingly, the respective homologs play a similar role in BMV translation and replication in yeast, and Hfq, a homolog of LSm1 in bacteria, is required for the replication of the (ϩ)RNA bacteriophage Qß (18). Furthermore, efficient retrotransposition of the yeast retrovirus-like elements Ty-1 and Ty-3 also depends on Dhh1, Lsm1, and Pat1 (19). One common theme for (ϩ)RNA viruses and retroviruses is that both need to regulate the transition of the genomic RNA from translation to encapsidation (20).…”

Section: Discussionmentioning

confidence: 99%

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Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates

Scheller

Mina

Galão

et al. 2009

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

128

166

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Inevitably, viruses depend on host factors for their multiplication. Here, we show that hepatitis C virus (HCV) RNA translation and replication depends on Rck/p54, LSm1, and PatL1, which regulate the fate of cellular mRNAs from translation to degradation in the 5 -3 -deadenylation-dependent mRNA decay pathway. The requirement of these proteins for efficient HCV RNA translation was linked to the 5 and 3 untranslated regions (UTRs) of the viral genome. Furthermore, LSm1-7 complexes specifically interacted with essential cis-acting HCV RNA elements located in the UTRs. These results bridge HCV life cycle requirements and highly conserved host proteins of cellular mRNA decay. The previously described role of these proteins in the replication of 2 other positive-strand RNA viruses, the plant brome mosaic virus and the bacteriophage Qß, pinpoint a weak spot that may be exploited to generate broad-spectrum antiviral drugs.deadenylation-dependent mRNA decay ͉ HCV ͉ host factors ͉ LSm1-7 ͉ Rck/p54

show abstract

Section: Discussionmentioning

confidence: 99%

“…These foci are sites where nontranslating mRNAs accumulate for different fates such as degradation, storage or returning to translation. Whether P-body formation itself is required for the HCV life cycle is an interesting issue (19) yet to be resolved in subsequent studies.…”

Section: Discussionmentioning

confidence: 99%

Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates

Scheller

Mina

Galão

et al. 2009

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

128

166

View full text Add to dashboard Cite

show abstract

“…Hosts use multiple antiviral mechanisms to restrict virus infection; formation of stress granules is an important antiviral response that limits virus replication by stalling viral protein synthesis (52,53). Activation of PKR is required for the formation of stress granules in response to virus infection (34)(35)(36)54).…”

Section: /2mentioning

confidence: 99%

NF90 Exerts Antiviral Activity through Regulation of PKR Phosphorylation and Stress Granules in Infected Cells

Wen

Huang

Mok

et al. 2014

The Journal of Immunology

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NF90 was shown to exhibit broad antiviral activity against several viruses, but detailed mechanisms remain unclear. In this study, we examined the molecular basis for the inhibitory effect of NF90 on virus replication mediated through protein kinase (PKR)-associated translational regulation. We first verified the interaction between NF90 and PKR in mammalian cells and showed that NF90 interacts with PKR through its C-terminal and that the interaction is independent of NF90 RNA-binding properties. We further showed that knockdown of NF90 resulted in significantly lower levels of PKR phosphorylation in response to dsRNA induction and influenza virus infection. We also showed that high concentrations of NF90 exhibit negative regulatory effects on PKR phosphorylation, presumably through competition for dsRNA via the C-terminal RNA-binding domain. PKR activation is essential for the formation of stress granules in response to dsRNA induction. Our results showed that NF90 is a component of stress granules. In NF90-knockdown cells, dsRNA treatment induced significantly lower levels of stress granules than in control cells. Further evidence for an NF90–PKR antiviral pathway was obtained using an NS1 mutated influenza A virus specifically attenuated in its ability to inhibit PKR activation. This mutant virus replicated indistinguishably from wild-type virus in NF90-knockdown cells, but not in scrambled control cells or Vero cells, indicating that NF90’s antiviral function occurs through interaction with PKR. Taken together, these results reveal a yet-to-be defined host antiviral mechanism in which NF90 upregulation of PKR phosphorylation restricts virus infection.

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“…As a result, the precise role of P-body granules in mRNA processing remains unclear. In mammalian cells, P-bodies have also been implicated in the microRNA-mediated inhibition of translation and in the replicative life cycle of several viruses (Liu et al 2005;Bhattacharyya et al 2006;Beckham and Parker 2008;Reineke and Lloyd 2013). Therefore, P-bodies, and perhaps other RNP granules, may be associated with different biological activities depending upon the particular proteins present in these structures.…”

mentioning

confidence: 99%

Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells

Shah¹,

Nostramo²,

Zhang³

et al. 2014

Genetics

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The cytoplasm of the eukaryotic cell is subdivided into distinct functional domains by the presence of a variety of membrane-bound organelles. The remaining aqueous space may be further partitioned by the regulated assembly of discrete ribonucleoprotein (RNP) complexes that contain particular proteins and messenger RNAs. These RNP granules are conserved structures whose importance is highlighted by studies linking them to human disorders like amyotrophic lateral sclerosis. However, relatively little is known about the diversity, composition, and physiological roles of these cytoplasmic structures. To begin to address these issues, we examined the cytoplasmic granules formed by a key set of signaling molecules, the protein kinases of the budding yeast Saccharomyces cerevisiae. Interestingly, a significant fraction of these proteins, almost 20%, was recruited to cytoplasmic foci specifically as cells entered into the G 0 -like quiescent state, stationary phase. Colocalization studies demonstrated that these foci corresponded to eight different granules, including four that had not been reported previously. All of these granules were found to rapidly disassemble upon the resumption of growth, and the presence of each was correlated with cell viability in the quiescent cultures. Finally, this work also identified new constituents of known RNP granules, including the well-characterized processing body and stress granule. The composition of these latter structures is therefore more varied than previously thought and could be an indicator of additional biological activities being associated with these complexes. Altogether, these observations indicate that quiescent yeast cells contain multiple distinct cytoplasmic granules that may make important contributions to their long-term survival.

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P Bodies, Stress Granules, and Viral Life Cycles

Cited by 205 publications

References 69 publications

Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates

Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates

NF90 Exerts Antiviral Activity through Regulation of PKR Phosphorylation and Stress Granules in Infected Cells

Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells

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