메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Polycomb repressive complex 2 facilitates the nuclear export of the influenza viral genome through the interaction with M1

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; POLYCOMB REPRESSIVE COMPLEX 2; PROTEIN BINDING; VIRUS RNA;

EID: 84988527324     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep33608     Document Type: Article
Times cited : (8)

References (49)
  • 1
    • 55849083076 scopus 로고    scopus 로고
    • Influenza A replication and host nuclear compartments: Many changes and many questions
    • Josset, L., Frobert, E., Rosa-Calatrava, M. Influenza A replication and host nuclear compartments: many changes and many questions. J. Clin. Virol. 43, 381-390 (2008).
    • (2008) J. Clin. Virol. , vol.43 , pp. 381-390
    • Josset, L.1    Frobert, E.2    Rosa-Calatrava, M.3
  • 2
    • 78651246115 scopus 로고    scopus 로고
    • Chromatin landscape: Methylation beyond transcription
    • Black, J. C., Whetstine, J. R. Chromatin landscape: methylation beyond transcription. Epigenetics 6, 9-15 (2011).
    • (2011) Epigenetics , vol.6 , pp. 9-15
    • Black, J.C.1    Whetstine, J.R.2
  • 3
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao, R. et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298, 1039-1043 (2002).
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1
  • 4
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang, H. et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 431, 873-878 (2004).
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1
  • 6
    • 84960982030 scopus 로고    scopus 로고
    • Influenza virus and the chromatin: Role of CHD1 chromatin remodeler on virus life cycle
    • Marcos-Villar, L., Pazo, A., Nieto, A. Influenza virus and the chromatin: Role of CHD1 chromatin remodeler on virus life cycle. J. Virol. 90, 3694-3707 (2016).
    • (2016) J. Virol. , vol.90 , pp. 3694-3707
    • Marcos-Villar, L.1    Pazo, A.2    Nieto, A.3
  • 7
    • 17444430403 scopus 로고    scopus 로고
    • Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II
    • Engelhardt, O. G., Smith, M., Fodor, E. Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II. J. Virol. 79, 5812-5818 (2005).
    • (2005) J. Virol. , vol.79 , pp. 5812-5818
    • Engelhardt, O.G.1    Smith, M.2    Fodor, E.3
  • 8
    • 36749077601 scopus 로고    scopus 로고
    • An influenza virus replicon system in yeast identified Tat-SF1 as a stimulatory host factor for viral RNA synthesis
    • Naito, T. et al. An influenza virus replicon system in yeast identified Tat-SF1 as a stimulatory host factor for viral RNA synthesis. Proc. Natl. Acad. Sci. USA 104, 18235-18240 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18235-18240
    • Naito, T.1
  • 10
    • 33646057735 scopus 로고    scopus 로고
    • Association of functional influenza viral proteins and RNAs with nuclear chromatin and sub-chromatin structure
    • Takizawa, N., Watanabe, K., Nouno, K., Kobayashi, N., Nagata, K. Association of functional influenza viral proteins and RNAs with nuclear chromatin and sub-chromatin structure. Microbes Infect. 8, 823-833 (2006).
    • (2006) Microbes Infect. , vol.8 , pp. 823-833
    • Takizawa, N.1    Watanabe, K.2    Nouno, K.3    Kobayashi, N.4    Nagata, K.5
  • 11
    • 81355154694 scopus 로고    scopus 로고
    • CHD6 chromatin remodeler is a negative modulator of influenza virus replication that relocates to inactive chromatin upon infection
    • Alfonso, R. et al. CHD6 chromatin remodeler is a negative modulator of influenza virus replication that relocates to inactive chromatin upon infection. Cell Microbiol. 13, 1894-1906 (2011).
    • (2011) Cell Microbiol. , vol.13 , pp. 1894-1906
    • Alfonso, R.1
  • 12
    • 84875783451 scopus 로고    scopus 로고
    • CHD6, a cellular repressor of influenza virus replication, is degraded in human alveolar epithelial cells and mice lungs during infection
    • Alfonso, R., Rodriguez, A., Rodriguez, P., Lutz, T., Nieto, A. CHD6, a cellular repressor of influenza virus replication, is degraded in human alveolar epithelial cells and mice lungs during infection. J. Virol. 87, 4534-4544 (2013).
    • (2013) J. Virol. , vol.87 , pp. 4534-4544
    • Alfonso, R.1    Rodriguez, A.2    Rodriguez, P.3    Lutz, T.4    Nieto, A.5
  • 13
    • 0034929835 scopus 로고    scopus 로고
    • Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B
    • Watanabe, K. et al. Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B. Virus Res. 77, 31-42 (2001).
    • (2001) Virus Res. , vol.77 , pp. 31-42
    • Watanabe, K.1
  • 14
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton, D. et al. Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J. Virol. 75, 408-419 (2001).
    • (2001) J. Virol. , vol.75 , pp. 408-419
    • Elton, D.1
  • 15
    • 0034671826 scopus 로고    scopus 로고
    • Influenza A virus NS2 protein mediates vRNP nuclear export through NESindependent interaction with hCRM1
    • Neumann, G., Hughes, M. T., Kawaoka, Y. Influenza A virus NS2 protein mediates vRNP nuclear export through NESindependent interaction with hCRM1. EMBO J. 19, 6751-6758 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6751-6758
    • Neumann, G.1    Hughes, M.T.2    Kawaoka, Y.3
  • 16
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • Noton, S. L. et al. Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J. Gen. Virol. 88, 2280-2290 (2007).
    • (2007) J. Gen. Virol. , vol.88 , pp. 2280-2290
    • Noton, S.L.1
  • 17
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin, F., Petit, I., Weissenhorn, W., Ruigrok, R. W. In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 281, 102-108 (2001).
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 18
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill, R. E., Talon, J., Palese, P. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J. 17, 288-296 (1998).
    • (1998) EMBO J. , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 19
    • 80053436121 scopus 로고    scopus 로고
    • Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting
    • Chase, G. P. et al. Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting. Plos Pathog. 7, e1002187 (2011).
    • (2011) Plos Pathog. , vol.7 , pp. e1002187
    • Chase, G.P.1
  • 20
    • 84869014044 scopus 로고    scopus 로고
    • YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules
    • Kawaguchi, A., Matsumoto, K., Nagata, K. YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules. J. Virol. 86, 11086-11095 (2012).
    • (2012) J. Virol. , vol.86 , pp. 11086-11095
    • Kawaguchi, A.1    Matsumoto, K.2    Nagata, K.3
  • 21
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex
    • Cao, R., Zhang, Y. SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol. Cell 15, 57-67 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 22
    • 84945186017 scopus 로고    scopus 로고
    • Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2
    • Jiao, L., Liu, X. Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2. Science 350, aac4383 (2015).
    • (2015) Science , vol.350 , pp. aac4383
    • Jiao, L.1    Liu, X.2
  • 23
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • Margueron, R. et al. Role of the polycomb protein EED in the propagation of repressive histone marks. Nature 461, 762-767 (2009).
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1
  • 24
    • 84922377030 scopus 로고    scopus 로고
    • SSX2 is a novel DNA-binding protein that antagonizes polycomb group body formation and gene repression
    • Gjerstorff, M. F. et al. SSX2 is a novel DNA-binding protein that antagonizes polycomb group body formation and gene repression. Nucleic Acids Res. 42, 11433-11446 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. 11433-11446
    • Gjerstorff, M.F.1
  • 25
    • 33846225576 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors deplete enhancer of zeste 2 and associated polycomb repressive complex 2 proteins in human acute leukemia cells
    • Fiskus, W. et al. Histone deacetylase inhibitors deplete enhancer of zeste 2 and associated polycomb repressive complex 2 proteins in human acute leukemia cells. Mol. Cancer Ther. 5, 3096-3104 (2006).
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 3096-3104
    • Fiskus, W.1
  • 26
    • 0037192823 scopus 로고    scopus 로고
    • Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus
    • Birbach, A. et al. Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus. J. Biol. Chem. 277, 10842-10851 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 10842-10851
    • Birbach, A.1
  • 27
    • 84870573126 scopus 로고    scopus 로고
    • EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
    • McCabe, M. T. et al. EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations. Nature 492, 108-112 (2012).
    • (2012) Nature , vol.492 , pp. 108-112
    • McCabe, M.T.1
  • 28
    • 35548976680 scopus 로고    scopus 로고
    • Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein
    • Momose, F., Kikuchi, Y., Komase, K., Morikawa, Y. Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein. Microbes Infect. 9, 1422-1433 (2007).
    • (2007) Microbes Infect. , vol.9 , pp. 1422-1433
    • Momose, F.1    Kikuchi, Y.2    Komase, K.3    Morikawa, Y.4
  • 29
    • 34948839944 scopus 로고    scopus 로고
    • Facultative heterochromatin: Is there a distinctive molecular signature Mol
    • Trojer, P., Reinberg, D. Facultative heterochromatin: is there a distinctive molecular signature Mol. Cell 28, 1-13 (2007).
    • (2007) Cell , vol.28 , pp. 1-13
    • Trojer, P.1    Reinberg, D.2
  • 30
    • 84956963448 scopus 로고    scopus 로고
    • Chromatin-prebound Crm1 recruits Nup98-HoxA9 fusion to induce aberrant expression of Hox cluster genes
    • Oka, M. et al. Chromatin-prebound Crm1 recruits Nup98-HoxA9 fusion to induce aberrant expression of Hox cluster genes. Elife 5, e09540 (2016).
    • (2016) Elife , vol.5 , pp. e09540
    • Oka, M.1
  • 31
    • 84922525901 scopus 로고    scopus 로고
    • A critical role for CRM1 in regulating HOXA gene transcription in CALM-AF10 leukemias
    • Conway, A. E., Haldeman, J. M., Wechsler, D. S., Lavau, C. P. A critical role for CRM1 in regulating HOXA gene transcription in CALM-AF10 leukemias. Leukemia 29, 423-432 (2015).
    • (2015) Leukemia , vol.29 , pp. 423-432
    • Conway, A.E.1    Haldeman, J.M.2    Wechsler, D.S.3    Lavau, C.P.4
  • 32
    • 84949131833 scopus 로고    scopus 로고
    • CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2
    • Hu, Y. et al. CHD3 facilitates vRNP nuclear export by interacting with NES1 of influenza A virus NS2. Cell Mol. Life Sci. 72, 971-982 (2015).
    • (2015) Cell Mol. Life Sci. , vol.72 , pp. 971-982
    • Hu, Y.1
  • 33
    • 84856431427 scopus 로고    scopus 로고
    • NuRD-mediated deacetylation of H3K27 facilitates recruitment of Polycomb Repressive Complex 2 to direct gene repression
    • Reynolds, N. et al. NuRD-mediated deacetylation of H3K27 facilitates recruitment of Polycomb Repressive Complex 2 to direct gene repression. EMBO J. 31, 593-605 (2012).
    • (2012) EMBO J. , vol.31 , pp. 593-605
    • Reynolds, N.1
  • 34
    • 84859589167 scopus 로고    scopus 로고
    • CHD3 protein recognizes and regulates methylated histone H3 lysines 4 and 27 over a subset of targets in the rice genome
    • Hu, Y. et al. CHD3 protein recognizes and regulates methylated histone H3 lysines 4 and 27 over a subset of targets in the rice genome. Proc. Natl. Acad. Sci. USA 109, 5773-5778 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5773-5778
    • Hu, Y.1
  • 35
    • 84860573037 scopus 로고    scopus 로고
    • The CHD3 remodeler PICKLE associates with genes enriched for trimethylation of histone H3 lysine 27
    • Zhang, H., Bishop, B., Ringenberg, W., Muir, W. M., Ogas, J. The CHD3 remodeler PICKLE associates with genes enriched for trimethylation of histone H3 lysine 27. Plant Physiol. 159, 418-432 (2012).
    • (2012) Plant Physiol. , vol.159 , pp. 418-432
    • Zhang, H.1    Bishop, B.2    Ringenberg, W.3    Muir, W.M.4    Ogas, J.5
  • 36
    • 84870795662 scopus 로고    scopus 로고
    • Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry
    • Hutchinson, E. C. et al. Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry. Plos Pathog. 8, e1002993 (2012).
    • (2012) Plos Pathog. , vol.8 , pp. e1002993
    • Hutchinson, E.C.1
  • 37
    • 84864297655 scopus 로고    scopus 로고
    • Independence of repressive histone marks and chromatin compaction during senescent heterochromatic layer formation
    • Chandra, T. et al. Independence of repressive histone marks and chromatin compaction during senescent heterochromatic layer formation. Mol. Cell 47, 203-214 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 203-214
    • Chandra, T.1
  • 38
    • 84892742949 scopus 로고    scopus 로고
    • PRC2-independent chromatin compaction and transcriptional repression in cancer
    • Vallot, C., Hérault, A., Boyle, S., Bickmore, W. A., Radvanyi, F. PRC2-independent chromatin compaction and transcriptional repression in cancer. Oncogene 34, 741-751 (2015).
    • (2015) Oncogene , vol.34 , pp. 741-751
    • Vallot, C.1    Hérault, A.2    Boyle, S.3    Bickmore, W.A.4    Radvanyi, F.5
  • 40
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • Everett, R. D., Chelbi-Alix, M. K. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89, 819-830 (2007).
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 41
    • 84879105224 scopus 로고    scopus 로고
    • Proximity to PML nuclear bodies regulates HIV-1 latency in CD4+ T cells
    • Lusic, M. et al. Proximity to PML nuclear bodies regulates HIV-1 latency in CD4+ T cells. Cell Host Microbe 13, 665-677 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 665-677
    • Lusic, M.1
  • 42
    • 0038205593 scopus 로고    scopus 로고
    • Localization of influenza virus proteins to nuclear dot 10 structures in influenza virus-infected cells
    • Sato, Y. et al. Localization of influenza virus proteins to nuclear dot 10 structures in influenza virus-infected cells. Virology 310, 29-40 (2003).
    • (2003) Virology , vol.310 , pp. 29-40
    • Sato, Y.1
  • 43
    • 59749103706 scopus 로고    scopus 로고
    • Immunofluorescence imaging of the influenza virus M1 protein is dependent on the fixation method
    • Shibata, T., Tanaka, T., Shimizu, K., Hayakawa, S., Kuroda, K. Immunofluorescence imaging of the influenza virus M1 protein is dependent on the fixation method. J. Virol. Methods 156, 162-165 (2009).
    • (2009) J. Virol. Methods , vol.156 , pp. 162-165
    • Shibata, T.1    Tanaka, T.2    Shimizu, K.3    Hayakawa, S.4    Kuroda, K.5
  • 44
    • 80052047427 scopus 로고    scopus 로고
    • Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein
    • Kawaguchi, A., Momose, F., Nagata, K. Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein. J. Virol. 85, 6197-6204 (2011).
    • (2011) J. Virol. , vol.85 , pp. 6197-6204
    • Kawaguchi, A.1    Momose, F.2    Nagata, K.3
  • 45
    • 33846491250 scopus 로고    scopus 로고
    • Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
    • Naito, T., Momose, F., Kawaguchi, A., Nagata, K. Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J. Virol. 81, 1339-1349 (2007).
    • (2007) J. Virol. , vol.81 , pp. 1339-1349
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 46
    • 84880368265 scopus 로고    scopus 로고
    • DNA replication-dependent binding of CTCF plays a critical role in adenovirus genome functions
    • Komatsu, T., Sekiya, T., Nagata, K. DNA replication-dependent binding of CTCF plays a critical role in adenovirus genome functions. Sci. Rep. 3, 2187 (2013).
    • (2013) Sci. Rep. , vol.3 , pp. 2187
    • Komatsu, T.1    Sekiya, T.2    Nagata, K.3
  • 47
    • 0028598355 scopus 로고
    • Regulation of influenza virus RNA polymerase activity by cellular and viral factors
    • Shimizu, K., Handa, H., Nakada, S., Nagata, K. Regulation of influenza virus RNA polymerase activity by cellular and viral factors. Nucleic Acids Res. 22, 5047-5053 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5047-5053
    • Shimizu, K.1    Handa, H.2    Nakada, S.3    Nagata, K.4
  • 48
    • 84919709326 scopus 로고    scopus 로고
    • Actin-myosin network is required for proper assembly of influenza virus particles
    • Kumakura, M., Kawaguchi, A., Nagata, K. Actin-myosin network is required for proper assembly of influenza virus particles. Virology 476, 141-150 (2015).
    • (2015) Virology , vol.476 , pp. 141-150
    • Kumakura, M.1    Kawaguchi, A.2    Nagata, K.3
  • 49
    • 0029656043 scopus 로고    scopus 로고
    • Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein
    • Watanabe, K., Handa, H., Mizumoto, K., Nagata, K. Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein. J. Virol. 70, 241-247 (1996).
    • (1996) J. Virol. , vol.70 , pp. 241-247
    • Watanabe, K.1    Handa, H.2    Mizumoto, K.3    Nagata, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.