The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.
Identifieur interne : 000227 ( Ncbi/Merge ); précédent : 000226; suivant : 000228The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.
Auteurs : Alan G. Goodman [États-Unis] ; Jennifer A. Smith ; Siddharth Balachandran ; Olivia Perwitasari ; Sean C. Proll ; Matthew J. Thomas ; Marcus J. Korth ; Glen N. Barber ; Leslie A. Schiff ; Michael G. KatzeSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), ARN viral (génétique), ARN viral (métabolisme), Animaux, Biosynthèse des protéines, Cellules cultivées, Facteur-2 d'initiation eucaryote (métabolisme), Modèles biologiques, Orthomyxoviridae (génétique), Orthomyxoviridae (physiologie), Phosphorylation, Protéines du choc thermique HSP40 (déficit), Protéines du choc thermique HSP40 (génétique), Protéines du choc thermique HSP40 (métabolisme), Protéines virales (biosynthèse), Reoviridae (génétique), Reoviridae (physiologie), Réplication virale, Souris, Souris knockout, Séquence nucléotidique, Virus de la stomatite vésiculeuse de type Indiana (génétique), Virus de la stomatite vésiculeuse de type Indiana (physiologie), eIF-2 Kinase (métabolisme).
- MESH :
- biosynthèse : Protéines virales.
- déficit : Protéines du choc thermique HSP40.
- génétique : ARN messager, ARN viral, Orthomyxoviridae, Protéines du choc thermique HSP40, Reoviridae, Virus de la stomatite vésiculeuse de type Indiana.
- métabolisme : ARN messager, ARN viral, Facteur-2 d'initiation eucaryote, Protéines du choc thermique HSP40, eIF-2 Kinase.
- physiologie : Orthomyxoviridae, Reoviridae, Virus de la stomatite vésiculeuse de type Indiana.
- Animaux, Biosynthèse des protéines, Cellules cultivées, Modèles biologiques, Phosphorylation, Réplication virale, Souris, Souris knockout, Séquence nucléotidique.
English descriptors
- KwdEn :
- Animals, Base Sequence, Cells, Cultured, Eukaryotic Initiation Factor-2 (metabolism), HSP40 Heat-Shock Proteins (deficiency), HSP40 Heat-Shock Proteins (genetics), HSP40 Heat-Shock Proteins (metabolism), Mice, Mice, Knockout, Models, Biological, Orthomyxoviridae (genetics), Orthomyxoviridae (physiology), Phosphorylation, Protein Biosynthesis, RNA, Messenger (genetics), RNA, Messenger (metabolism), RNA, Viral (genetics), RNA, Viral (metabolism), Reoviridae (genetics), Reoviridae (physiology), Vesicular stomatitis Indiana virus (genetics), Vesicular stomatitis Indiana virus (physiology), Viral Proteins (biosynthesis), Virus Replication, eIF-2 Kinase (metabolism).
- MESH :
- chemical , biosynthesis : Viral Proteins.
- chemical , deficiency : HSP40 Heat-Shock Proteins.
- chemical , genetics : HSP40 Heat-Shock Proteins, RNA, Messenger, RNA, Viral.
- chemical , metabolism : Eukaryotic Initiation Factor-2, HSP40 Heat-Shock Proteins, RNA, Messenger, RNA, Viral, eIF-2 Kinase.
- genetics : Orthomyxoviridae, Reoviridae, Vesicular stomatitis Indiana virus.
- physiology : Orthomyxoviridae, Reoviridae, Vesicular stomatitis Indiana virus.
- Animals, Base Sequence, Cells, Cultured, Mice, Mice, Knockout, Models, Biological, Phosphorylation, Protein Biosynthesis, Virus Replication.
Abstract
We previously hypothesized that efficient translation of influenza virus mRNA requires the recruitment of P58(IPK), the cellular inhibitor of PKR, an interferon-induced kinase that targets the eukaryotic translation initiation factor eIF2alpha. P58(IPK) also inhibits PERK, an eIF2alpha kinase that is localized in the endoplasmic reticulum (ER) and induced during ER stress. The ability of P58(IPK) to interact with and inhibit multiple eIF2alpha kinases suggests it is a critical regulator of both cellular and viral mRNA translation. In this study, we sought to definitively define the role of P58(IPK) during viral infection of mammalian cells. Using mouse embryo fibroblasts from P58(IPK-/-) mice, we demonstrated that the absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation. The absence of P58(IPK) also resulted in decreased vesicular stomatitis virus replication but enhanced reovirus yields. In cells lacking the P58(IPK) target, PKR, the trends were reversed-eIF2alpha phosphorylation was decreased, and influenza virus mRNA translation was increased. Although P58(IPK) also inhibits PERK, the presence or absence of this kinase had little effect on influenza virus mRNA translation, despite reduced levels of eIF2alpha phosphorylation in cells lacking PERK. Finally, we showed that influenza virus protein synthesis and viral mRNA levels decrease in cells that express a constitutively active, nonphosphorylatable eIF2alpha. Taken together, our results support a model in which P58(IPK) regulates influenza virus mRNA translation and infection through a PKR-mediated mechanism which is independent of PERK.
DOI: 10.1128/JVI.02151-06
PubMed: 17166899
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000816
- to stream PubMed, to step Curation: 000813
- to stream PubMed, to step Checkpoint: 000769
Links to Exploration step
pubmed:17166899Le document en format XML
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<front><div type="abstract" xml:lang="en">We previously hypothesized that efficient translation of influenza virus mRNA requires the recruitment of P58(IPK), the cellular inhibitor of PKR, an interferon-induced kinase that targets the eukaryotic translation initiation factor eIF2alpha. P58(IPK) also inhibits PERK, an eIF2alpha kinase that is localized in the endoplasmic reticulum (ER) and induced during ER stress. The ability of P58(IPK) to interact with and inhibit multiple eIF2alpha kinases suggests it is a critical regulator of both cellular and viral mRNA translation. In this study, we sought to definitively define the role of P58(IPK) during viral infection of mammalian cells. Using mouse embryo fibroblasts from P58(IPK-/-) mice, we demonstrated that the absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation. The absence of P58(IPK) also resulted in decreased vesicular stomatitis virus replication but enhanced reovirus yields. In cells lacking the P58(IPK) target, PKR, the trends were reversed-eIF2alpha phosphorylation was decreased, and influenza virus mRNA translation was increased. Although P58(IPK) also inhibits PERK, the presence or absence of this kinase had little effect on influenza virus mRNA translation, despite reduced levels of eIF2alpha phosphorylation in cells lacking PERK. Finally, we showed that influenza virus protein synthesis and viral mRNA levels decrease in cells that express a constitutively active, nonphosphorylatable eIF2alpha. Taken together, our results support a model in which P58(IPK) regulates influenza virus mRNA translation and infection through a PKR-mediated mechanism which is independent of PERK.</div>
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<ArticleTitle>The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.</ArticleTitle>
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<Abstract><AbstractText>We previously hypothesized that efficient translation of influenza virus mRNA requires the recruitment of P58(IPK), the cellular inhibitor of PKR, an interferon-induced kinase that targets the eukaryotic translation initiation factor eIF2alpha. P58(IPK) also inhibits PERK, an eIF2alpha kinase that is localized in the endoplasmic reticulum (ER) and induced during ER stress. The ability of P58(IPK) to interact with and inhibit multiple eIF2alpha kinases suggests it is a critical regulator of both cellular and viral mRNA translation. In this study, we sought to definitively define the role of P58(IPK) during viral infection of mammalian cells. Using mouse embryo fibroblasts from P58(IPK-/-) mice, we demonstrated that the absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation. The absence of P58(IPK) also resulted in decreased vesicular stomatitis virus replication but enhanced reovirus yields. In cells lacking the P58(IPK) target, PKR, the trends were reversed-eIF2alpha phosphorylation was decreased, and influenza virus mRNA translation was increased. Although P58(IPK) also inhibits PERK, the presence or absence of this kinase had little effect on influenza virus mRNA translation, despite reduced levels of eIF2alpha phosphorylation in cells lacking PERK. Finally, we showed that influenza virus protein synthesis and viral mRNA levels decrease in cells that express a constitutively active, nonphosphorylatable eIF2alpha. Taken together, our results support a model in which P58(IPK) regulates influenza virus mRNA translation and infection through a PKR-mediated mechanism which is independent of PERK.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Goodman</LastName>
<ForeName>Alan G</ForeName>
<Initials>AG</Initials>
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<ForeName>Jennifer A</ForeName>
<Initials>JA</Initials>
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<ArticleId IdType="doi">10.1128/JVI.02151-06</ArticleId>
<ArticleId IdType="pmc">PMC1865913</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>J Biol Chem. 1993 Oct 25;268(30):22223-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8226725</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1994 Apr;14(4):2331-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7511204</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1995 Jan;69(1):552-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7527088</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1995 Dec 1;214(1):222-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8525619</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1995 Dec 15;14(24):6095-106</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8557029</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1996 Aug;16(8):4172-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8754816</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1997 Apr 14;230(2):217-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9143277</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1997 May 26;232(1):62-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9185589</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1998 May;18(5):2431-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9566864</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1998 Dec 1;17(23):6888-902</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9843495</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1999 Feb 5;274(6):3797-803</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9920933</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6694-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10359774</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1999 Jul;19(7):4757-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10373525</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Dec;78(23):12747-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15542627</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2004 Dec;24(23):10161-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15542827</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 2004 Dec;10(12 Suppl):S82-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15577936</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Feb;79(3):1379-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15650164</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Semin Cell Dev Biol. 2005 Feb;16(1):3-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15659334</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Feb;79(4):2240-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15681426</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Diabetes. 2005 Apr;54(4):1074-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15793246</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Microbiol. 2005 Apr;13(4):159-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15817385</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FASEB J. 2005 Sep;19(11):1510-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16006626</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mech Ageing Dev. 2000 Mar 13;114(2):123-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10799709</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1990 Aug;87(16):6208-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1696720</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Immunity. 2000 Jul;13(1):129-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10933401</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Sep;74(17):7989-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10933707</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Dec;74(24):11566-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11090154</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2001 Jun;7(6):1153-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11430819</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2001 Jun;7(6):1165-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11430820</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2002 Feb 22;108(4):545-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11909525</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 May;76(9):4162-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11932381</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 Aug;76(15):7430-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12097555</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 Oct;76(19):9588-99</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12208938</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15920-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12446838</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 May 2;278(18):15558-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12601012</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1991 Aug;114(3):401-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1650370</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Enzyme. 1990;44(1-4):265-77</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2133654</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1992 May 5;267(13):9383-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1577765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1992 Jul 15;267(20):14238-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1378438</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1992 Nov;66(11):6408-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1328674</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1992 Dec;66(12):6878-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1433498</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2005 Oct 5;24(19):3470-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16148948</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Feb;80(4):2019-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16439558</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2006 Apr 19;25(8):1730-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16601681</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Res. 2006 Jul;119(1):111-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16630668</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2006 Aug 25;126(4):727-39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16923392</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2006 Oct 5;443(7111):578-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17006449</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Dev Cell. 2003 May;4(5):651-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12737801</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2004 Jan 14;23(1):169-79</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14713949</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2004 Jul 8;430(6996):209-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15241415</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1975 Dec;16(6):1464-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1202245</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1979 Apr;76(4):1618-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">287003</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1981 Mar;23(3):847-58</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6261960</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1986 May;6(5):1741-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3785177</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1987 Mar;6(3):689-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3582371</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1988 Jan;62(1):246-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3275434</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1988 Mar 31;332(6163):462-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3352747</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1988 Oct;62(10):3710-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3418783</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1988 Dec;62(12):4594-604</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2460637</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1990 Jul 27;62(2):379-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1695551</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2000 May;5(5):897-904</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10882126</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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