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Volumn 6, Issue 6, 2014, Pages 1026-1036

Marburgvirus Hijacks Nrf2-Dependent Pathway by Targeting Nrf2-Negative Regulator Keap1

Author keywords

[No Author keywords available]

Indexed keywords

KELCH LIKE ECH ASSOCIATED PROTEIN 1; PROTEIN VP24; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; VIRUS PROTEIN; COMPLEMENTARY DNA; HEME OXYGENASE 1; KARYOPHERIN; KARYOPHERIN ALPHA; KARYOPHERIN BETA; PROTEIN VP40; TRANSCRIPTION FACTOR GAL4; CYTOSKELETON PROTEIN; KEAP1 PROTEIN, HUMAN; KEAP1 PROTEIN, MOUSE; PROTEIN BINDING; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84897095146     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.02.027     Document Type: Article
Times cited : (77)

References (53)
  • 2
    • 27144503018 scopus 로고    scopus 로고
    • VP24 of Marburg virus influences formation of infectious particles
    • Bamberg S., Kolesnikova L., Möller P., Klenk H.D., Becker S. VP24 of Marburg virus influences formation of infectious particles. J.Virol. 2005, 79:13421-13433.
    • (2005) J.Virol. , vol.79 , pp. 13421-13433
    • Bamberg, S.1    Kolesnikova, L.2    Möller, P.3    Klenk, H.D.4    Becker, S.5
  • 3
    • 76849085285 scopus 로고    scopus 로고
    • Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway
    • Burdette D., Olivarez M., Waris G. Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway. J.Gen. Virol. 2010, 91:681-690.
    • (2010) J.Gen. Virol. , vol.91 , pp. 681-690
    • Burdette, D.1    Olivarez, M.2    Waris, G.3
  • 6
    • 0009447935 scopus 로고    scopus 로고
    • Filoviruses University of Texas Medical Branch, Galveston, S. Baron (Ed.)
    • Feldmann H., Klenk H.D. Filoviruses. Medical Microbiology 1996, University of Texas Medical Branch, Galveston. 4th edition. S. Baron (Ed.).
    • (1996) Medical Microbiology
    • Feldmann, H.1    Klenk, H.D.2
  • 8
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa M., Xiong Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol. Cell. Biol. 2005, 25:162-171.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 11
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
    • Hayes J.D., McMahon M. NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends Biochem. Sci. 2009, 34:176-188.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 12
    • 79959715844 scopus 로고    scopus 로고
    • Minigenomes, transcription and replication competent virus-like particles and beyond: reverse genetics systems for filoviruses and other negative stranded hemorrhagic fever viruses
    • Hoenen T., Groseth A., de Kok-Mercado F., Kuhn J.H., Wahl-Jensen V. Minigenomes, transcription and replication competent virus-like particles and beyond: reverse genetics systems for filoviruses and other negative stranded hemorrhagic fever viruses. Antiviral Res. 2011, 91:195-208.
    • (2011) Antiviral Res. , vol.91 , pp. 195-208
    • Hoenen, T.1    Groseth, A.2    de Kok-Mercado, F.3    Kuhn, J.H.4    Wahl-Jensen, V.5
  • 13
    • 79957945853 scopus 로고    scopus 로고
    • Viral-mediated inhibition of antioxidant enzymes contributes to the pathogenesis of severe respiratory syncytial virus bronchiolitis
    • Hosakote Y.M., Jantzi P.D., Esham D.L., Spratt H., Kurosky A., Casola A., Garofalo R.P. Viral-mediated inhibition of antioxidant enzymes contributes to the pathogenesis of severe respiratory syncytial virus bronchiolitis. Am. J. Respir. Crit. Care Med. 2011, 183:1550-1560.
    • (2011) Am. J. Respir. Crit. Care Med. , vol.183 , pp. 1550-1560
    • Hosakote, Y.M.1    Jantzi, P.D.2    Esham, D.L.3    Spratt, H.4    Kurosky, A.5    Casola, A.6    Garofalo, R.P.7
  • 14
    • 0036670360 scopus 로고    scopus 로고
    • The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein
    • Huang Y., Xu L., Sun Y., Nabel G.J. The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein. Mol. Cell 2002, 10:307-316.
    • (2002) Mol. Cell , vol.10 , pp. 307-316
    • Huang, Y.1    Xu, L.2    Sun, Y.3    Nabel, G.J.4
  • 15
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 1999, 13:76-86.
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 16
    • 1942520367 scopus 로고    scopus 로고
    • Nrf2 signaling in coordinated activation of antioxidant gene expression
    • Jaiswal A.K. Nrf2 signaling in coordinated activation of antioxidant gene expression. Free Radic. Biol. Med. 2004, 36:1199-1207.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1199-1207
    • Jaiswal, A.K.1
  • 18
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang M.I., Kobayashi A., Wakabayashi N., Kim S.G., Yamamoto M. Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc. Natl. Acad. Sci. USA 2004, 101:2046-2051.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 19
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A., Kang M.I., Okawa H., Ohtsuji M., Zenke Y., Chiba T., Igarashi K., Yamamoto M. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell. Biol. 2004, 24:7130-7139.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 20
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
    • Kobayashi A., Kang M.I., Watai Y., Tong K.I., Shibata T., Uchida K., Yamamoto M. Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol. Cell. Biol. 2006, 26:221-229.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3    Tong, K.I.4    Shibata, T.5    Uchida, K.6    Yamamoto, M.7
  • 22
    • 11144244006 scopus 로고    scopus 로고
    • Crystal structure of the Kelch domain of human Keap1
    • Li X., Zhang D., Hannink M., Beamer L.J. Crystal structure of the Kelch domain of human Keap1. J.Biol. Chem. 2004, 279:54750-54758.
    • (2004) J.Biol. Chem. , vol.279 , pp. 54750-54758
    • Li, X.1    Zhang, D.2    Hannink, M.3    Beamer, L.J.4
  • 23
    • 19944412632 scopus 로고    scopus 로고
    • Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1
    • Li X., Zhang D., Hannink M., Beamer L.J. Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:2346-2348.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2346-2348
    • Li, X.1    Zhang, D.2    Hannink, M.3    Beamer, L.J.4
  • 24
    • 22244478316 scopus 로고    scopus 로고
    • Outbreak of Marburg hemorrhagic fever in Angola: a review of the history of the disease and its biological aspects
    • Ligon B.L. Outbreak of Marburg hemorrhagic fever in Angola: a review of the history of the disease and its biological aspects. Semin. Pediatr. Infect. Dis. 2005, 16:219-224.
    • (2005) Semin. Pediatr. Infect. Dis. , vol.16 , pp. 219-224
    • Ligon, B.L.1
  • 25
    • 33747606306 scopus 로고    scopus 로고
    • Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
    • Lo S.C., Li X., Henzl M.T., Beamer L.J., Hannink M. Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. EMBO J. 2006, 25:3605-3617.
    • (2006) EMBO J. , vol.25 , pp. 3605-3617
    • Lo, S.C.1    Li, X.2    Henzl, M.T.3    Beamer, L.J.4    Hannink, M.5
  • 26
    • 84867034260 scopus 로고    scopus 로고
    • Role of nrf2 in oxidative stress and toxicity
    • Ma Q. Role of nrf2 in oxidative stress and toxicity. Annu. Rev. Pharmacol. Toxicol. 2013, 53:401-426.
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 401-426
    • Ma, Q.1
  • 27
    • 4043053773 scopus 로고    scopus 로고
    • Pathogenesis of filoviral haemorrhagic fevers
    • Mahanty S., Bray M. Pathogenesis of filoviral haemorrhagic fevers. Lancet Infect. Dis. 2004, 4:487-498.
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 487-498
    • Mahanty, S.1    Bray, M.2
  • 28
    • 73849109409 scopus 로고    scopus 로고
    • Ebolavirus VP24 binding to karyopherins is required for inhibition of interferon signaling
    • Mateo M., Reid S.P., Leung L.W., Basler C.F., Volchkov V.E. Ebolavirus VP24 binding to karyopherins is required for inhibition of interferon signaling. J.Virol. 2010, 84:1169-1175.
    • (2010) J.Virol. , vol.84 , pp. 1169-1175
    • Mateo, M.1    Reid, S.P.2    Leung, L.W.3    Basler, C.F.4    Volchkov, V.E.5
  • 32
    • 65649141970 scopus 로고    scopus 로고
    • Potential factors induced by filoviruses that lead to immune supression
    • Mohamadzadeh M. Potential factors induced by filoviruses that lead to immune supression. Curr. Mol. Med. 2009, 9:174-185.
    • (2009) Curr. Mol. Med. , vol.9 , pp. 174-185
    • Mohamadzadeh, M.1
  • 33
    • 2342511435 scopus 로고    scopus 로고
    • Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway
    • Motohashi H., Katsuoka F., Engel J.D., Yamamoto M. Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway. Proc. Natl. Acad. Sci. USA 2004, 101:6379-6384.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6379-6384
    • Motohashi, H.1    Katsuoka, F.2    Engel, J.D.3    Yamamoto, M.4
  • 34
    • 77649261371 scopus 로고    scopus 로고
    • Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains
    • Ogura T., Tong K.I., Mio K., Maruyama Y., Kurokawa H., Sato C., Yamamoto M. Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains. Proc. Natl. Acad. Sci. USA 2010, 107:2842-2847.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2842-2847
    • Ogura, T.1    Tong, K.I.2    Mio, K.3    Maruyama, Y.4    Kurokawa, H.5    Sato, C.6    Yamamoto, M.7
  • 35
    • 42449150854 scopus 로고    scopus 로고
    • Structural insights into the similar modes of Nrf2 transcription factor recognition by the cytoplasmic repressor Keap1
    • Padmanabhan B., Tong K.I., Kobayashi A., Yamamoto M., Yokoyama S. Structural insights into the similar modes of Nrf2 transcription factor recognition by the cytoplasmic repressor Keap1. J.Synchrotron Radiat. 2008, 15:273-276.
    • (2008) J.Synchrotron Radiat. , vol.15 , pp. 273-276
    • Padmanabhan, B.1    Tong, K.I.2    Kobayashi, A.3    Yamamoto, M.4    Yokoyama, S.5
  • 38
    • 37149040796 scopus 로고    scopus 로고
    • Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1
    • Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F. Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1. J.Virol. 2007, 81:13469-13477.
    • (2007) J.Virol. , vol.81 , pp. 13469-13477
    • Reid, S.P.1    Valmas, C.2    Martinez, O.3    Sanchez, F.M.4    Basler, C.F.5
  • 40
    • 58149181985 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced expression of NAD(P)H:quinone oxidoreductase 1 and heme oxygenase-1 protects against excessive inflammatory responses in human monocytes
    • Rushworth S.A., MacEwan D.J., O'Connell M.A. Lipopolysaccharide-induced expression of NAD(P)H:quinone oxidoreductase 1 and heme oxygenase-1 protects against excessive inflammatory responses in human monocytes. J.Immunol. 2008, 181:6730-6737.
    • (2008) J.Immunol. , vol.181 , pp. 6730-6737
    • Rushworth, S.A.1    MacEwan, D.J.2    O'Connell, M.A.3
  • 41
    • 4544228226 scopus 로고    scopus 로고
    • Analysis of human peripheral blood samples from fatal and nonfatal cases of Ebola (Sudan) hemorrhagic fever: cellular responses, virus load, and nitric oxide levels
    • Sanchez A., Lukwiya M., Bausch D., Mahanty S., Sanchez A.J., Wagoner K.D., Rollin P.E. Analysis of human peripheral blood samples from fatal and nonfatal cases of Ebola (Sudan) hemorrhagic fever: cellular responses, virus load, and nitric oxide levels. J.Virol. 2004, 78:10370-10377.
    • (2004) J.Virol. , vol.78 , pp. 10370-10377
    • Sanchez, A.1    Lukwiya, M.2    Bausch, D.3    Mahanty, S.4    Sanchez, A.J.5    Wagoner, K.D.6    Rollin, P.E.7
  • 43
    • 0029782304 scopus 로고    scopus 로고
    • Oxidative stress during viral infection: a review
    • Schwarz K.B. Oxidative stress during viral infection: a review. Free Radic. Biol. Med. 1996, 21:641-649.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 641-649
    • Schwarz, K.B.1
  • 45
    • 35449002458 scopus 로고    scopus 로고
    • Preclinical evaluation of targeting the Nrf2 pathway by triterpenoids (CDDO-Im andCDDO-Me) for protection from LPS-induced inflammatory response and reactive oxygen species in human peripheral blood mononuclear cells and neutrophils
    • Thimmulappa R.K., Fuchs R.J., Malhotra D., Scollick C., Traore K., Bream J.H., Trush M.A., Liby K.T., Sporn M.B., Kensler T.W., et al. Preclinical evaluation of targeting the Nrf2 pathway by triterpenoids (CDDO-Im andCDDO-Me) for protection from LPS-induced inflammatory response and reactive oxygen species in human peripheral blood mononuclear cells and neutrophils. Antioxid. Redox. Signal. 2007, 9:1963-1970.
    • (2007) Antioxid. Redox. Signal. , vol.9 , pp. 1963-1970
    • Thimmulappa, R.K.1    Fuchs, R.J.2    Malhotra, D.3    Scollick, C.4    Traore, K.5    Bream, J.H.6    Trush, M.A.7    Liby, K.T.8    Sporn, M.B.9    Kensler, T.W.10
  • 46
    • 33344463325 scopus 로고    scopus 로고
    • Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model
    • Tong K.I., Katoh Y., Kusunoki H., Itoh K., Tanaka T., Yamamoto M. Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. Mol. Cell. Biol. 2006, 26:2887-2900.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2887-2900
    • Tong, K.I.1    Katoh, Y.2    Kusunoki, H.3    Itoh, K.4    Tanaka, T.5    Yamamoto, M.6
  • 47
    • 35648970026 scopus 로고    scopus 로고
    • Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response
    • Tong K.I., Padmanabhan B., Kobayashi A., Shang C., Hirotsu Y., Yokoyama S., Yamamoto M. Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response. Mol. Cell. Biol. 2007, 27:7511-7521.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7511-7521
    • Tong, K.I.1    Padmanabhan, B.2    Kobayashi, A.3    Shang, C.4    Hirotsu, Y.5    Yokoyama, S.6    Yamamoto, M.7
  • 48
    • 79955407974 scopus 로고    scopus 로고
    • Marburg virus VP40 antagonizes interferon signaling in a species-specific manner
    • Valmas C., Basler C.F. Marburg virus VP40 antagonizes interferon signaling in a species-specific manner. J.Virol. 2011, 85:4309-4317.
    • (2011) J.Virol. , vol.85 , pp. 4309-4317
    • Valmas, C.1    Basler, C.F.2
  • 52
    • 0027407071 scopus 로고
    • Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein
    • Will C., Mühlberger E., Linder D., Slenczka W., Klenk H.D., Feldmann H. Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein. J.Virol. 1993, 67:1203-1210.
    • (1993) J.Virol. , vol.67 , pp. 1203-1210
    • Will, C.1    Mühlberger, E.2    Linder, D.3    Slenczka, W.4    Klenk, H.D.5    Feldmann, H.6
  • 53
    • 67449090404 scopus 로고    scopus 로고
    • Nrf2 is involved in inhibiting Tat-induced HIV-1 long terminal repeat transactivation
    • Zhang H.S., Li H.Y., Zhou Y., Wu M.R., Zhou H.S. Nrf2 is involved in inhibiting Tat-induced HIV-1 long terminal repeat transactivation. Free Radic. Biol. Med. 2009, 47:261-268.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 261-268
    • Zhang, H.S.1    Li, H.Y.2    Zhou, Y.3    Wu, M.R.4    Zhou, H.S.5


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