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Volumn 8, Issue 6, 2013, Pages

Eukaryotic Initiation Factor 4H Is under Transcriptional Control of p65/NF-κB

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INITIATION FACTOR; INITIATION FACTOR 4A; PROTEIN EIF4H; RNA HELICASE; SYNAPTOTAGMIN I; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG;

EID: 84979963779     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066087     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV, (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11: 113-127.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 3
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F
    • Rogers GW Jr, Richter NJ, Lima WF, Merrick WC, (2001) Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J Biol Chem 276: 30914-30922.
    • (2001) J Biol Chem , vol.276 , pp. 30914-30922
    • Rogers Jr., G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 4
    • 59049092956 scopus 로고    scopus 로고
    • Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation
    • Marintchev A, Edmonds KA, Marintcheva B, Hendrickson E, Oberer M, et al. (2009) Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation. Cell 136: 447-460.
    • (2009) Cell , vol.136 , pp. 447-460
    • Marintchev, A.1    Edmonds, K.A.2    Marintcheva, B.3    Hendrickson, E.4    Oberer, M.5
  • 5
    • 0028126506 scopus 로고
    • PHAS-I as a link between mitogen-activated protein kinase and translation initiation
    • Lin TA, Kong X, Haystead TA, Pause A, Belsham G, et al. (1994) PHAS-I as a link between mitogen-activated protein kinase and translation initiation. Science 266: 653-656.
    • (1994) Science , vol.266 , pp. 653-656
    • Lin, T.A.1    Kong, X.2    Haystead, T.A.3    Pause, A.4    Belsham, G.5
  • 6
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause A, Belsham GJ, Gingras AC, Donze O, Lin TA, et al. (1994) Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371: 762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5
  • 7
    • 33750325725 scopus 로고    scopus 로고
    • S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth
    • Dorrello NV, Peschiaroli A, Guardavaccaro D, Colburn NH, Sherman NE, et al. (2006) S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth. Science 314: 467-471.
    • (2006) Science , vol.314 , pp. 467-471
    • Dorrello, N.V.1    Peschiaroli, A.2    Guardavaccaro, D.3    Colburn, N.H.4    Sherman, N.E.5
  • 8
    • 33745570504 scopus 로고    scopus 로고
    • The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity
    • Shahbazian D, Roux PP, Mieulet V, Cohen MS, Raught B, et al. (2006) The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity. Embo J 25: 2781-2791.
    • (2006) Embo J , vol.25 , pp. 2781-2791
    • Shahbazian, D.1    Roux, P.P.2    Mieulet, V.3    Cohen, M.S.4    Raught, B.5
  • 9
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud CG, (2005) eIF2 and the control of cell physiology. Semin Cell Dev Biol 16: 3-12.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 10
    • 34548483411 scopus 로고    scopus 로고
    • Mechanisms of translational deregulation in human tumors and therapeutic intervention strategies
    • Bilanges B, Stokoe D, (2007) Mechanisms of translational deregulation in human tumors and therapeutic intervention strategies. Oncogene 26: 5973-5990.
    • (2007) Oncogene , vol.26 , pp. 5973-5990
    • Bilanges, B.1    Stokoe, D.2
  • 11
    • 85047696004 scopus 로고    scopus 로고
    • Translation initiation and its deregulation during tumorigenesis
    • Watkins SJ, Norbury CJ, (2002) Translation initiation and its deregulation during tumorigenesis. Br J Cancer 86: 1023-1027.
    • (2002) Br J Cancer , vol.86 , pp. 1023-1027
    • Watkins, S.J.1    Norbury, C.J.2
  • 12
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG, (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136: 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 13
    • 0036725994 scopus 로고    scopus 로고
    • Translation initiation in cancer: a novel target for therapy
    • Meric F, Hunt KK, (2002) Translation initiation in cancer: a novel target for therapy. Mol Cancer Ther 1: 971-979.
    • (2002) Mol Cancer Ther , vol.1 , pp. 971-979
    • Meric, F.1    Hunt, K.K.2
  • 14
    • 54949147176 scopus 로고    scopus 로고
    • New regulators of NF-kappaB in inflammation
    • Ghosh S, Hayden MS, (2008) New regulators of NF-kappaB in inflammation. Nat Rev Immunol 8: 837-848.
    • (2008) Nat Rev Immunol , vol.8 , pp. 837-848
    • Ghosh, S.1    Hayden, M.S.2
  • 15
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-kappaB transcription factors in the immune system
    • Vallabhapurapu S, Karin M, (2009) Regulation and function of NF-kappaB transcription factors in the immune system. Annu Rev Immunol 27: 693-733.
    • (2009) Annu Rev Immunol , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 16
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li Q, Verma IM, (2002) NF-kappaB regulation in the immune system. Nat Rev Immunol 2: 725-734.
    • (2002) Nat Rev Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 17
    • 0025812292 scopus 로고
    • Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity
    • Haskill S, Beg AA, Tompkins SM, Morris JS, Yurochko AD, et al. (1991) Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity. Cell 65: 1281-1289.
    • (1991) Cell , vol.65 , pp. 1281-1289
    • Haskill, S.1    Beg, A.A.2    Tompkins, S.M.3    Morris, J.S.4    Yurochko, A.D.5
  • 18
    • 0033565217 scopus 로고    scopus 로고
    • Expression of a dominant-negative mutant inhibitor-kappaBalpha of nuclear factor-kappaB in human head and neck squamous cell carcinoma inhibits survival, proinflammatory cytokine expression, and tumor growth in vivo
    • Duffey DC, Chen Z, Dong G, Ondrey FG, Wolf JS, et al. (1999) Expression of a dominant-negative mutant inhibitor-kappaBalpha of nuclear factor-kappaB in human head and neck squamous cell carcinoma inhibits survival, proinflammatory cytokine expression, and tumor growth in vivo. Cancer Res 59: 3468-3474.
    • (1999) Cancer Res , vol.59 , pp. 3468-3474
    • Duffey, D.C.1    Chen, Z.2    Dong, G.3    Ondrey, F.G.4    Wolf, J.S.5
  • 19
    • 0033581013 scopus 로고    scopus 로고
    • Potent and stable attenuation of live-HIV-1 by gain of a proteolysis-resistant inhibitor of NF-kappaB (IkappaB-alphaS32/36A) and the implications for vaccine development
    • Quinto I, Mallardo M, Baldassarre F, Scala G, Englund G, et al. (1999) Potent and stable attenuation of live-HIV-1 by gain of a proteolysis-resistant inhibitor of NF-kappaB (IkappaB-alphaS32/36A) and the implications for vaccine development. J Biol Chem 274: 17567-17572.
    • (1999) J Biol Chem , vol.274 , pp. 17567-17572
    • Quinto, I.1    Mallardo, M.2    Baldassarre, F.3    Scala, G.4    Englund, G.5
  • 20
    • 78650745895 scopus 로고    scopus 로고
    • An alternative splicing isoform of eukaryotic initiation factor 4H promotes tumorigenesis in vivo and is a potential therapeutic target for human cancer
    • Wu D, Matsushita K, Matsubara H, Nomura F, Tomonaga T, (2011) An alternative splicing isoform of eukaryotic initiation factor 4H promotes tumorigenesis in vivo and is a potential therapeutic target for human cancer. Int J Cancer 128: 1018-1030.
    • (2011) Int J Cancer , vol.128 , pp. 1018-1030
    • Wu, D.1    Matsushita, K.2    Matsubara, H.3    Nomura, F.4    Tomonaga, T.5
  • 21
    • 18144378095 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication in primary human monocytes by the IkappaB-alphaS32/36A repressor of NF-kappaB
    • Palmieri C, Trimboli F, Puca A, Fiume G, Scala G, et al. (2004) Inhibition of HIV-1 replication in primary human monocytes by the IkappaB-alphaS32/36A repressor of NF-kappaB. Retrovirology 1: 45.
    • (2004) Retrovirology , vol.1 , pp. 45
    • Palmieri, C.1    Trimboli, F.2    Puca, A.3    Fiume, G.4    Scala, G.5
  • 22
    • 79960846480 scopus 로고    scopus 로고
    • Structural and functional insights into IkappaB-alpha/HIV-1 Tat interaction
    • Vitagliano L, Fiume G, Scognamiglio PL, Doti N, Cannavo R, et al. (2011) Structural and functional insights into IkappaB-alpha/HIV-1 Tat interaction. Biochimie 93: 1592-1600.
    • (2011) Biochimie , vol.93 , pp. 1592-1600
    • Vitagliano, L.1    Fiume, G.2    Scognamiglio, P.L.3    Doti, N.4    Cannavo, R.5
  • 23
    • 37549034692 scopus 로고    scopus 로고
    • IkappaB-alpha represses the transcriptional activity of the HIV-1 Tat transactivator by promoting its nuclear export
    • Puca A, Fiume G, Palmieri C, Trimboli F, Olimpico F, et al. (2007) IkappaB-alpha represses the transcriptional activity of the HIV-1 Tat transactivator by promoting its nuclear export. J Biol Chem 282: 37146-37157.
    • (2007) J Biol Chem , vol.282 , pp. 37146-37157
    • Puca, A.1    Fiume, G.2    Palmieri, C.3    Trimboli, F.4    Olimpico, F.5
  • 24
    • 79955750270 scopus 로고    scopus 로고
    • Mass spectrometry-based identification of the tumor antigen UN1 as the transmembrane CD43 sialoglycoprotein
    • de Laurentiis A, Gaspari M, Palmieri C, Falcone C, Iaccino E, et al. (2011) Mass spectrometry-based identification of the tumor antigen UN1 as the transmembrane CD43 sialoglycoprotein. Mol Cell Proteomics 10: M111 007898.
    • (2011) Mol Cell Proteomics , vol.10
    • de Laurentiis, A.1    Gaspari, M.2    Palmieri, C.3    Falcone, C.4    Iaccino, E.5
  • 25
    • 79959257186 scopus 로고    scopus 로고
    • Btk regulation in human and mouse B cells via protein kinase C phosphorylation of IBtkgamma
    • Janda E, Palmieri C, Pisano A, Pontoriero M, Iaccino E, et al. (2011) Btk regulation in human and mouse B cells via protein kinase C phosphorylation of IBtkgamma. Blood 117: 6520-6531.
    • (2011) Blood , vol.117 , pp. 6520-6531
    • Janda, E.1    Palmieri, C.2    Pisano, A.3    Pontoriero, M.4    Iaccino, E.5
  • 26
    • 84861550676 scopus 로고    scopus 로고
    • Design and Characterization of a Peptide Mimotope of the HIV-1 gp120 Bridging Sheet
    • Schiavone M, Fiume G, Caivano A, de Laurentiis A, Falcone C, et al. (2012) Design and Characterization of a Peptide Mimotope of the HIV-1 gp120 Bridging Sheet. Int J Mol Sci 13: 5674-5699.
    • (2012) Int J Mol Sci , vol.13 , pp. 5674-5699
    • Schiavone, M.1    Fiume, G.2    Caivano, A.3    de Laurentiis, A.4    Falcone, C.5
  • 27
    • 48649111199 scopus 로고    scopus 로고
    • FK506 can activate transforming growth factor-beta signalling in vascular smooth muscle cells and promote proliferation
    • Giordano A, Romano S, Mallardo M, D'Angelillo A, Calì G, et al. (2008) FK506 can activate transforming growth factor-beta signalling in vascular smooth muscle cells and promote proliferation. Cardiovasc Res. 1 79(3): 519-26.
    • (2008) Cardiovasc Res , vol.79 , Issue.3 , pp. 519-526
    • Giordano, A.1    Romano, S.2    Mallardo, M.3    D'Angelillo, A.4    Calì, G.5
  • 28
    • 84860371902 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Tat activates NF-kappaB via physical interaction with IkappaB-alpha and p65
    • Fiume G, Vecchio E, De Laurentiis A, Trimboli F, Palmieri C, et al. (2012) Human immunodeficiency virus-1 Tat activates NF-kappaB via physical interaction with IkappaB-alpha and p65. Nucleic Acids Res 40: 3548-3562.
    • (2012) Nucleic Acids Res , vol.40 , pp. 3548-3562
    • Fiume, G.1    Vecchio, E.2    De Laurentiis, A.3    Trimboli, F.4    Palmieri, C.5
  • 29
    • 70449713316 scopus 로고    scopus 로고
    • Computational analysis and in vivo validation of a microRNA encoded by the IBTK gene, a regulator of B-lymphocytes differentiation and survival
    • Fiume G, Rossi A, Di Salle E, Spatuzza C, Mallardo M, et al. (2009) Computational analysis and in vivo validation of a microRNA encoded by the IBTK gene, a regulator of B-lymphocytes differentiation and survival. Comput Biol Chem 33: 434-439.
    • (2009) Comput Biol Chem , vol.33 , pp. 434-439
    • Fiume, G.1    Rossi, A.2    Di Salle, E.3    Spatuzza, C.4    Mallardo, M.5
  • 30
    • 48349089940 scopus 로고    scopus 로고
    • Physical and functional characterization of the genetic locus of IBtk, an inhibitor of Bruton's tyrosine kinase: evidence for three protein isoforms of IBtk
    • Spatuzza C, Schiavone M, Di Salle E, Janda E, Sardiello M, et al. (2008) Physical and functional characterization of the genetic locus of IBtk, an inhibitor of Bruton's tyrosine kinase: evidence for three protein isoforms of IBtk. Nucleic Acids Res 36: 4402-4416.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4402-4416
    • Spatuzza, C.1    Schiavone, M.2    Di Salle, E.3    Janda, E.4    Sardiello, M.5
  • 31
    • 0033544894 scopus 로고    scopus 로고
    • Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H
    • Richter NJ, Rogers GW Jr, Hensold JO, Merrick WC, (1999) Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H. J Biol Chem 274: 35415-35424.
    • (1999) J Biol Chem , vol.274 , pp. 35415-35424
    • Richter, N.J.1    Rogers Jr., G.W.2    Hensold, J.O.3    Merrick, W.C.4
  • 32
    • 0023894279 scopus 로고
    • Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA
    • Abramson RD, Dever TE, Merrick WC, (1988) Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA. J Biol Chem 263: 6016-6019.
    • (1988) J Biol Chem , vol.263 , pp. 6016-6019
    • Abramson, R.D.1    Dever, T.E.2    Merrick, W.C.3
  • 33
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
    • Rogers GW Jr, Richter NJ, Merrick WC, (1999) Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J Biol Chem 274: 12236-12244.
    • (1999) J Biol Chem , vol.274 , pp. 12236-12244
    • Rogers Jr., G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 34
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen F, Edery I, Meerovitch K, Dever TE, Merrick WC, et al. (1990) Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol Cell Biol 10: 1134-1144.
    • (1990) Mol Cell Biol , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5
  • 35
    • 0021875798 scopus 로고
    • ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors
    • Ray BK, Lawson TG, Kramer JC, Cladaras MH, Grifo JA, et al. (1985) ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors. J Biol Chem 260: 7651-7658.
    • (1985) J Biol Chem , vol.260 , pp. 7651-7658
    • Ray, B.K.1    Lawson, T.G.2    Kramer, J.C.3    Cladaras, M.H.4    Grifo, J.A.5
  • 36
    • 0021270173 scopus 로고
    • RNA-stimulated ATPase activity of eukaryotic initiation factors
    • Grifo JA, Abramson RD, Satler CA, Merrick WC, (1984) RNA-stimulated ATPase activity of eukaryotic initiation factors. J Biol Chem 259: 8648-8654.
    • (1984) J Biol Chem , vol.259 , pp. 8648-8654
    • Grifo, J.A.1    Abramson, R.D.2    Satler, C.A.3    Merrick, W.C.4
  • 37
    • 58149202128 scopus 로고    scopus 로고
    • Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls
    • Baud V, Karin M, (2009) Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls. Nat Rev Drug Discov 8: 33-40.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 33-40
    • Baud, V.1    Karin, M.2
  • 38
    • 77749323441 scopus 로고    scopus 로고
    • Control of cell survival and proliferation by mammalian eukaryotic initiation factor 4B
    • Shahbazian D, Parsyan A, Petroulakis E, Topisirovic I, Martineau Y, et al. (2010) Control of cell survival and proliferation by mammalian eukaryotic initiation factor 4B. Mol Cell Biol 30: 1478-1485.
    • (2010) Mol Cell Biol , vol.30 , pp. 1478-1485
    • Shahbazian, D.1    Parsyan, A.2    Petroulakis, E.3    Topisirovic, I.4    Martineau, Y.5


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