메뉴 건너뛰기




Volumn 15, Issue 12, 2015, Pages 1983-1994

Human cytomegalovirus TRS1 protein associates with the 7-methylguanosine mRNA cap and facilitates translation

Author keywords

Microbiology; PKR; Translational control; Virology

Indexed keywords

7 METHYLGUANOSINE; MESSENGER RNA; PROTEIN KINASE R; TRS1 PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; 7-METHYLGUANOSINE; CAP BINDING PROTEIN; GUANOSINE; TRS1 PROTEIN, HUMAN HERPESVIRUS 5; VIRAL PROTEIN; VIRUS RNA;

EID: 84931009518     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400616     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 84867636500 scopus 로고    scopus 로고
    • Host translation at the nexus of infection and immunity
    • Mohr, I., Sonenberg, N., Host translation at the nexus of infection and immunity. Cell Host Microbe 2012, 12, 470-483.
    • (2012) Cell Host Microbe , vol.12 , pp. 470-483
    • Mohr, I.1    Sonenberg, N.2
  • 3
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras, A. C., Raught, B., Sonenberg, N., eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Ann. Rev. Biochem. 1999, 68, 913-963.
    • (1999) Ann. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 5
    • 0035231288 scopus 로고    scopus 로고
    • Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis
    • Clemens, M. J., Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis. Progress Mol. Subcell. Biol. 2001, 27, 57-89.
    • (2001) Progress Mol. Subcell. Biol. , vol.27 , pp. 57-89
    • Clemens, M.J.1
  • 6
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman, N. J., Cristea, I. M., Terhune, S. S., Rout, M. P. et al., Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 2008, 3, 253-262.
    • (2008) Cell Host Microbe , vol.3 , pp. 253-262
    • Moorman, N.J.1    Cristea, I.M.2    Terhune, S.S.3    Rout, M.P.4
  • 7
    • 0346995213 scopus 로고    scopus 로고
    • Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1
    • Child, S. J., Hakki, M., DeNiro, K. L., Geballe, A. P., Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1. J. Virol. 2004, 78, 197-205.
    • (2004) J. Virol. , vol.78 , pp. 197-205
    • Child, S.J.1    Hakki, M.2    De Niro, K.L.3    Geballe, A.P.4
  • 8
    • 19944372421 scopus 로고    scopus 로고
    • Double-stranded RNA binding by human cytomegalovirus pTRS1
    • Hakki, M., Geballe, A. P., Double-stranded RNA binding by human cytomegalovirus pTRS1. J. Virol. 2005, 79, 7311-7318.
    • (2005) J. Virol. , vol.79 , pp. 7311-7318
    • Hakki, M.1    Geballe, A.P.2
  • 9
    • 33751224189 scopus 로고    scopus 로고
    • Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1
    • Hakki, M., Marshall, E. E., DeNiro, K. L., Geballe, A. P., Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1. J. Virol. 2006, 80, 11817-11826.
    • (2006) J. Virol. , vol.80 , pp. 11817-11826
    • Hakki, M.1    Marshall, E.E.2    De Niro, K.L.3    Geballe, A.P.4
  • 10
    • 66149085620 scopus 로고    scopus 로고
    • Essential role for either TRS1 or IRS1 in human cytomegalovirus replication
    • Marshall, E. E., Bierle, C. J., Brune, W., Geballe, A. P., Essential role for either TRS1 or IRS1 in human cytomegalovirus replication. J. Virol. 2009, 83, 4112-4120.
    • (2009) J. Virol. , vol.83 , pp. 4112-4120
    • Marshall, E.E.1    Bierle, C.J.2    Brune, W.3    Geballe, A.P.4
  • 11
    • 84859597567 scopus 로고    scopus 로고
    • Poly(A) binding protein abundance regulates eukaryotic translation initiation factor 4F assembly in human cytomegalovirus-infected cells
    • McKinney, C., Perez, C., Mohr, I., Poly(A) binding protein abundance regulates eukaryotic translation initiation factor 4F assembly in human cytomegalovirus-infected cells. Proc. Natl. Acad. Sci. USA 2012, 109, 5627-5632.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5627-5632
    • McKinney, C.1    Perez, C.2    Mohr, I.3
  • 12
    • 20744448501 scopus 로고    scopus 로고
    • Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells
    • Walsh, D., Perez, C., Notary, J., Mohr, I., Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J. Virol. 2005, 79, 8057-8064.
    • (2005) J. Virol. , vol.79 , pp. 8057-8064
    • Walsh, D.1    Perez, C.2    Notary, J.3    Mohr, I.4
  • 13
    • 79952844950 scopus 로고    scopus 로고
    • The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection
    • Clippinger, A. J., Maguire, T. G., Alwine, J. C., The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection. J. Virol. 2011, 85, 3930-3939.
    • (2011) J. Virol. , vol.85 , pp. 3930-3939
    • Clippinger, A.J.1    Maguire, T.G.2    Alwine, J.C.3
  • 14
    • 84892454259 scopus 로고    scopus 로고
    • Differential role for host translation factors in host and viral protein synthesis during human cytomegalovirus infection
    • Lenarcic, E. M., Ziehr, B., DeLeon, G., Mitchell, D., Moorman, N. J., Differential role for host translation factors in host and viral protein synthesis during human cytomegalovirus infection. J. Virol. 2014, 88, 1473-1483.
    • (2014) J. Virol. , vol.88 , pp. 1473-1483
    • Lenarcic, E.M.1    Ziehr, B.2    De Leon, G.3    Mitchell, D.4    Moorman, N.J.5
  • 15
    • 29744432654 scopus 로고    scopus 로고
    • Production of infectious human cytomegalovirus virions is inhibited by drugs that disrupt calcium homeostasis in the endoplasmic reticulum
    • Isler, J. A., Maguire, T. G., Alwine, J. C., Production of infectious human cytomegalovirus virions is inhibited by drugs that disrupt calcium homeostasis in the endoplasmic reticulum. J. Virol. 2005, 79, 15388-15397.
    • (2005) J. Virol. , vol.79 , pp. 15388-15397
    • Isler, J.A.1    Maguire, T.G.2    Alwine, J.C.3
  • 16
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler, J. A., Skalet, A. H., Alwine, J. C., Human cytomegalovirus infection activates and regulates the unfolded protein response. J. Virol. 2005, 79, 6890-6899.
    • (2005) J. Virol. , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 17
    • 0036171607 scopus 로고    scopus 로고
    • Construction of a self-excisable bacterial artificial chromosome containing the human cytomegalovirus genome and mutagenesis of the diploid TRL/IRL13 gene
    • Yu, D., Smith, G. A., Enquist, L. W., Shenk, T., Construction of a self-excisable bacterial artificial chromosome containing the human cytomegalovirus genome and mutagenesis of the diploid TRL/IRL13 gene. J. Virol. 2002, 76, 2316-2328.
    • (2002) J. Virol. , vol.76 , pp. 2316-2328
    • Yu, D.1    Smith, G.A.2    Enquist, L.W.3    Shenk, T.4
  • 18
    • 33744980686 scopus 로고    scopus 로고
    • Quantitative proteomics identifies Gemin5, a scaffolding protein involved in ribonucleoprotein assembly, as a novel partner for eukaryotic initiation factor 4E
    • Fierro-Monti, I., Mohammed, S., Matthiesen, R., Santoro, R. et al., Quantitative proteomics identifies Gemin5, a scaffolding protein involved in ribonucleoprotein assembly, as a novel partner for eukaryotic initiation factor 4E. J. Proteome Res. 2006, 5, 1367-1378.
    • (2006) J. Proteome Res. , vol.5 , pp. 1367-1378
    • Fierro-Monti, I.1    Mohammed, S.2    Matthiesen, R.3    Santoro, R.4
  • 19
    • 77954671476 scopus 로고    scopus 로고
    • Human cytomegalovirus UL29/28 protein interacts with components of the NuRD complex which promote accumulation of immediate-early RNA
    • Terhune, S. S., Moorman, N. J., Cristea, I. M., Savaryn, J. P. et al., Human cytomegalovirus UL29/28 protein interacts with components of the NuRD complex which promote accumulation of immediate-early RNA. PLoS Pathogens 2010, 6, e1000965.
    • (2010) PLoS Pathogens , vol.6 , pp. e1000965
    • Terhune, S.S.1    Moorman, N.J.2    Cristea, I.M.3    Savaryn, J.P.4
  • 20
    • 77954485440 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein
    • Cristea, I. M., Moorman, N. J., Terhune, S. S., Cuevas, C. D. et al., Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein. J. Virol. 2010, 84, 7803-7814.
    • (2010) J. Virol. , vol.84 , pp. 7803-7814
    • Cristea, I.M.1    Moorman, N.J.2    Terhune, S.S.3    Cuevas, C.D.4
  • 21
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha, N., Anderson, P., Mammalian stress granules and processing bodies. Methods Enzymol. 2007, 431, 61-81.
    • (2007) Methods Enzymol. , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 22
    • 77951790602 scopus 로고    scopus 로고
    • A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation
    • Moorman, N. J., Sharon-Friling, R., Shenk, T., Cristea, I. M., A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation. Mol. Cell. Proteomics 2010, 9, 851-860.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 851-860
    • Moorman, N.J.1    Sharon-Friling, R.2    Shenk, T.3    Cristea, I.M.4
  • 23
    • 0031014705 scopus 로고    scopus 로고
    • Characterization of the human cytomegalovirus irs1 and trs1 genes: a second immediate-early transcription unit within irs1 whose product antagonizes transcriptional activation
    • Romanowski, M. J., Shenk, T., Characterization of the human cytomegalovirus irs1 and trs1 genes: a second immediate-early transcription unit within irs1 whose product antagonizes transcriptional activation. J. Virol. 1997, 71, 1485-1496.
    • (1997) J. Virol. , vol.71 , pp. 1485-1496
    • Romanowski, M.J.1    Shenk, T.2
  • 24
    • 84892749369 scopus 로고    scopus 로고
    • Genetic screens in human cells using the CRISPR-Cas9 system
    • Wang, T., Wei, J. J., Sabatini, D. M., Lander, E. S., Genetic screens in human cells using the CRISPR-Cas9 system. Science 2014, 343, 80-84.
    • (2014) Science , vol.343 , pp. 80-84
    • Wang, T.1    Wei, J.J.2    Sabatini, D.M.3    Lander, E.S.4
  • 25
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter, J. D., Sonenberg, N., Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 2005, 433, 477-480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 26
    • 0027969151 scopus 로고
    • A nuclear cap binding protein complex involved in pre-mRNA splicing
    • Izaurralde, E., Lewis, J., McGuigan, C., Jankowska, M. et al., A nuclear cap binding protein complex involved in pre-mRNA splicing. Cell 1994, 78, 657-668.
    • (1994) Cell , vol.78 , pp. 657-668
    • Izaurralde, E.1    Lewis, J.2    McGuigan, C.3    Jankowska, M.4
  • 27
    • 70349193390 scopus 로고    scopus 로고
    • Identification of gemin5 as a novel 7-methylguanosine cap-binding protein
    • Bradrick, S. S., Gromeier, M., Identification of gemin5 as a novel 7-methylguanosine cap-binding protein. PloS One 2009, 4, e7030.
    • (2009) PloS One , vol.4 , pp. e7030
    • Bradrick, S.S.1    Gromeier, M.2
  • 28
    • 84878900854 scopus 로고    scopus 로고
    • Double-stranded RNA binding by the human cytomegalovirus PKR antagonist TRS1
    • Bierle, C. J., Semmens, K. M., Geballe, A. P., Double-stranded RNA binding by the human cytomegalovirus PKR antagonist TRS1. Virology 2013, 442, 28-37.
    • (2013) Virology , vol.442 , pp. 28-37
    • Bierle, C.J.1    Semmens, K.M.2    Geballe, A.P.3
  • 29
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan, J. R., Parker, R., Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 2009, 36, 932-941.
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 30
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson, P., Kedersha, N., Stress granules: the Tao of RNA triage. Trends Biochem. Sci. 2008, 33, 141-150.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 31
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition
    • Dey, M., Cao, C., Dar, A. C., Tamura, T. et al., Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition. Cell 2005, 122, 901-913.
    • (2005) Cell , vol.122 , pp. 901-913
    • Dey, M.1    Cao, C.2    Dar, A.C.3    Tamura, T.4
  • 32
    • 79551687500 scopus 로고    scopus 로고
    • Regulation of innate immunity through RNA structure and the protein kinase PKR
    • Nallagatla, S. R., Toroney, R., Bevilacqua, P. C., Regulation of innate immunity through RNA structure and the protein kinase PKR. Curr. Opin. Struct. Biol. 2011, 21, 119-127.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 119-127
    • Nallagatla, S.R.1    Toroney, R.2    Bevilacqua, P.C.3
  • 34
    • 0031899816 scopus 로고    scopus 로고
    • Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2
    • Romano, P. R., Garcia-Barrio, M. T., Zhang, X., Wang, Q. et al., Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2. Mol. Cell. Biol. 1998, 18, 2282-2297.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2282-2297
    • Romano, P.R.1    Garcia-Barrio, M.T.2    Zhang, X.3    Wang, Q.4
  • 35
    • 0023136956 scopus 로고
    • Translational control mediated by eucaryotic initiation factor-2 is restricted to specific mRNAs in transfected cells
    • Kaufman, R. J., Murtha, P., Translational control mediated by eucaryotic initiation factor-2 is restricted to specific mRNAs in transfected cells. Mol. Cell. Biol. 1987, 7, 1568-1571.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1568-1571
    • Kaufman, R.J.1    Murtha, P.2
  • 36
    • 0024582782 scopus 로고
    • The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs
    • Kaufman, R. J., Davies, M. V., Pathak, V. K., Hershey, J. W., The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs. Mol. Cell. Biol. 1989, 9, 946-958.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 946-958
    • Kaufman, R.J.1    Davies, M.V.2    Pathak, V.K.3    Hershey, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.