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Volumn 112, Issue 7, 2008, Pages 2750-2760

Igbpl is part of a positive feedback loop in stem cell factor-dependent, selective mRNA translation initiation inhibiting erythroid differentiation

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN BINDING PROTEIN 1; INITIATION FACTOR 4E; INITIATION FACTOR 4E BINDING PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPROTEIN PHOSPHATASE 2A; S6 KINASE; STEM CELL FACTOR; UNCLASSIFIED DRUG; ERYTHROPOIETIN; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; SIGNAL PEPTIDE; TRANSFORMING GROWTH FACTOR BETA;

EID: 53449102851     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-01-133140     Document Type: Article
Times cited : (34)

References (81)
  • 1
    • 0035377208 scopus 로고    scopus 로고
    • Establishment of normal, terminally differentiating mouse erythroid progenitors: Molecular characterization by cDNA arrays
    • Dolznig H. Boulme F, Stangl K. et al. Establishment of normal, terminally differentiating mouse erythroid progenitors: molecular characterization by cDNA arrays. FASEB J. 2001;15:1442-1444.
    • (2001) FASEB J , vol.15 , pp. 1442-1444
    • Dolznig, H.1    Boulme, F.2    Stangl, K.3
  • 2
    • 0035927590 scopus 로고    scopus 로고
    • Leukemic transformation of normal murine erythroid progenitors: V- and c-ErbB act through signaling pathways activated by the EpoR and c-Kit in stress erythropoiesis
    • von Lindern M, Deiner EM, Dolznig H. et al. Leukemic transformation of normal murine erythroid progenitors: v- and c-ErbB act through signaling pathways activated by the EpoR and c-Kit in stress erythropoiesis. Oncogene. 2001;20:3651-3664.
    • (2001) Oncogene , vol.20 , pp. 3651-3664
    • von Lindern, M.1    Deiner, E.M.2    Dolznig, H.3
  • 3
    • 0032758352 scopus 로고    scopus 로고
    • The glucocorticoid receptor is required for stress erythropoiesis
    • Bauer A, Tranche F, Wessely O, et al. The glucocorticoid receptor is required for stress erythropoiesis. Genes Dev. 1999;13:2996-3002.
    • (1999) Genes Dev , vol.13 , pp. 2996-3002
    • Bauer, A.1    Tranche, F.2    Wessely, O.3
  • 4
    • 0029957757 scopus 로고    scopus 로고
    • Interaction of stem cell factor and its receptor c-kit mediates lodgment and acute expansion of hematopoietic cells in the murine spleen
    • Broudy VC, Lin NL, Priestley GV, Nocka K, Wolf NS. Interaction of stem cell factor and its receptor c-kit mediates lodgment and acute expansion of hematopoietic cells in the murine spleen. Blood. 1996;88:75-81.
    • (1996) Blood , vol.88 , pp. 75-81
    • Broudy, V.C.1    Lin, N.L.2    Priestley, G.V.3    Nocka, K.4    Wolf, N.S.5
  • 5
    • 0030980933 scopus 로고    scopus 로고
    • Identification of a novel pathway important for proliferation and differentiation of primary erythroid progenitors
    • Klingmuller U, Wu H, Hsiao JG, et al. Identification of a novel pathway important for proliferation and differentiation of primary erythroid progenitors. Proc Natl Acad Sci U S A. 1997;94:3016-3021.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3016-3021
    • Klingmuller, U.1    Wu, H.2    Hsiao, J.G.3
  • 6
    • 0033890345 scopus 로고    scopus 로고
    • Stem cell factor and erythropoietin inhibit apoptosis of human erythroid progenitor cells through different signalling pathways
    • Sui X, Krantz SB, Zhao ZJ. Stem cell factor and erythropoietin inhibit apoptosis of human erythroid progenitor cells through different signalling pathways. Br J Haematol. 2000;110:63-70.
    • (2000) Br J Haematol , vol.110 , pp. 63-70
    • Sui, X.1    Krantz, S.B.2    Zhao, Z.J.3
  • 7
    • 0034057327 scopus 로고    scopus 로고
    • Erythroid cells rendered erythropoietin independent by infection with Friend spleen focus-forming virus show constitutive activation of phosphatidylinositol 3-kinase and Akt kinase: Involvement of insulin receptor substrate-related adapter proteins
    • Nishigaki K, Hanson G, Ohashi T, Thompson D, Muszynski K, Ruscetti S. Erythroid cells rendered erythropoietin independent by infection with Friend spleen focus-forming virus show constitutive activation of phosphatidylinositol 3-kinase and Akt kinase: involvement of insulin receptor substrate-related adapter proteins. J Virol. 2000; 74:3037-3045.
    • (2000) J Virol , vol.74 , pp. 3037-3045
    • Nishigaki, K.1    Hanson, G.2    Ohashi, T.3    Thompson, D.4    Muszynski, K.5    Ruscetti, S.6
  • 8
    • 13044269652 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is involved in the protection of primary cultured human erythroid precursor cells from apoptosis
    • Haseyama Y, Sawada K, Oda A, et al. Phosphatidylinositol 3-kinase is involved in the protection of primary cultured human erythroid precursor cells from apoptosis. Blood. 1999;94:1568-1577.
    • (1999) Blood , vol.94 , pp. 1568-1577
    • Haseyama, Y.1    Sawada, K.2    Oda, A.3
  • 9
    • 1642580499 scopus 로고    scopus 로고
    • FoxO3a regulates erythroid differentiation and induces BTG1. an activator of protein arginine methyl transferase 1
    • Bakker WJ, Blazquez-Domingo M, Kolbus A, et al. FoxO3a regulates erythroid differentiation and induces BTG1. an activator of protein arginine methyl transferase 1. J Cell Biol. 2004;164:175-184.
    • (2004) J Cell Biol , vol.164 , pp. 175-184
    • Bakker, W.J.1    Blazquez-Domingo, M.2    Kolbus, A.3
  • 10
    • 25444502964 scopus 로고    scopus 로고
    • Translation initiation factor 4E inhibits differentiation of erythroid progenitors
    • Blazquez-Domingo M, Grech G, von Lindern M. Translation initiation factor 4E inhibits differentiation of erythroid progenitors. Mol Cell Biol. 2005; 25:8496-8506.
    • (2005) Mol Cell Biol , vol.25 , pp. 8496-8506
    • Blazquez-Domingo, M.1    Grech, G.2    von Lindern, M.3
  • 11
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee AR, Manning BD, Roux PP, Cantley LC, Blenis J. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr Biol. 2003; 13:1259-1268.
    • (2003) Curr Biol , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 12
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki K, Li Y, Xu T, Guan KL. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 2003;17:1829-1834.
    • (2003) Genes Dev , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 13
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signaling and the control of translation
    • Dufner A, Thomas G. Ribosomal S6 kinase signaling and the control of translation. Exp Cell Res. 1999;253:100-109.
    • (1999) Exp Cell Res , vol.253 , pp. 100-109
    • Dufner, A.1    Thomas, G.2
  • 14
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
    • Gingras AC, Gygi SP, Raught B, et al. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism. Genes Dev. 1999;13:1422-1437.
    • (1999) Genes Dev , vol.13 , pp. 1422-1437
    • Gingras, A.C.1    Gygi, S.P.2    Raught, B.3
  • 15
    • 27744569843 scopus 로고    scopus 로고
    • mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz MK, Ballif BA, Gygi SP, Blenis J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell. 2005;123:569-580.
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 16
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras AC, Raught B, Sonenberg N. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 2001:15:807-826.
    • (2001) Genes Dev , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 17
    • 0032834055 scopus 로고    scopus 로고
    • elF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N. elF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem. 1999;68:913-963.
    • (1999) Annu Rev Biochem , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 18
    • 34247118887 scopus 로고    scopus 로고
    • Signalling to translation: How signal transduction pathways control the protein synthetic machinery
    • Proud CG. Signalling to translation: how signal transduction pathways control the protein synthetic machinery. Biochem J. 2007;403:217-234.
    • (2007) Biochem J , vol.403 , pp. 217-234
    • Proud, C.G.1
  • 19
    • 29144444289 scopus 로고    scopus 로고
    • A second look at cellular mRNA sequences said to function as internal ribosome entry sites
    • Kozak M. A second look at cellular mRNA sequences said to function as internal ribosome entry sites. Nucleic Acids Res. 2005;33:6593-6602.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6593-6602
    • Kozak, M.1
  • 20
    • 0023124676 scopus 로고
    • Regulated phosphorylation and low abundance of HeLa cell initiation factor elF-4F suggest a role in translational control: Heat shock effects on elF-4F
    • Duncan R, Milburn SC, Hershey JW. Regulated phosphorylation and low abundance of HeLa cell initiation factor elF-4F suggest a role in translational control: heat shock effects on elF-4F J Biol Chem. 1987;262:380-388.
    • (1987) J Biol Chem , vol.262 , pp. 380-388
    • Duncan, R.1    Milburn, S.C.2    Hershey, J.W.3
  • 21
    • 0032054816 scopus 로고    scopus 로고
    • The mRNA 5'-binding protein elF4E and control of cell growth
    • Sonenberg N, Gingras A-C. The mRNA 5'-binding protein elF4E and control of cell growth. Curr Opin Cell Biol. 1998;10:268-275.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 268-275
    • Sonenberg, N.1    Gingras, A.-C.2
  • 22
    • 0026723117 scopus 로고
    • mRNAs containing extensive secondary structure in their 5' noncoding region translate efficiently in cells overexpressing initiation factor elF-4E
    • Koromilas AE, Lazaris-Karatzas A, Sonenberg N. mRNAs containing extensive secondary structure in their 5' noncoding region translate efficiently in cells overexpressing initiation factor elF-4E. EMBO J. 1992;11:4153-4158.
    • (1992) EMBO J , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 24
    • 15044340650 scopus 로고    scopus 로고
    • Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins
    • Wang X, Beugnet A, Murakami M, Yamanaka S, Proud GG. Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins. Mol Cell Biol. 2005;25:2558-2572.
    • (2005) Mol Cell Biol , vol.25 , pp. 2558-2572
    • Wang, X.1    Beugnet, A.2    Murakami, M.3    Yamanaka, S.4    Proud, G.G.5
  • 25
    • 0030984108 scopus 로고    scopus 로고
    • B cell receptorassociated protein alpha4 displays rapamycinsensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • Murata K, Wu J, Brautigan DL. B cell receptorassociated protein alpha4 displays rapamycinsensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc Natl Acad Sci U S A. 1997;94:10624-10629.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 26
    • 0032528434 scopus 로고    scopus 로고
    • Ig receptor binding protein 1 (alpha4) is associated with a rapamycinsensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A
    • Inui S, Sanjo H, Maeda K, Yamamoto H, Miyamoto E, Sakaguchi N. Ig receptor binding protein 1 (alpha4) is associated with a rapamycinsensitive signal transduction in lymphocytes through direct binding to the catalytic subunit of protein phosphatase 2A. Blood. 1998;92:539-546.
    • (1998) Blood , vol.92 , pp. 539-546
    • Inui, S.1    Sanjo, H.2    Maeda, K.3    Yamamoto, H.4    Miyamoto, E.5    Sakaguchi, N.6
  • 27
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
    • Di Como CJ, Arndt KT. Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev. 1996;10:1904-1916.
    • (1996) Genes Dev , vol.10 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 28
    • 7444233154 scopus 로고    scopus 로고
    • The PP2A-associated protein alpha4 is an essential inhibitor of apoptosis
    • Kong M, Fox CJ, Mu J, et al. The PP2A-associated protein alpha4 is an essential inhibitor of apoptosis. Science. 2004;306:695-698.
    • (2004) Science , vol.306 , pp. 695-698
    • Kong, M.1    Fox, C.J.2    Mu, J.3
  • 29
    • 33750076984 scopus 로고    scopus 로고
    • The alpha4 regulatory subunit exerts opposing allosteric effects on protein phosphatases PP6 and PP2A
    • Prickett TD, Brautigan DL. The alpha4 regulatory subunit exerts opposing allosteric effects on protein phosphatases PP6 and PP2A. J Biol Chem. 2006:281:30503-30511.
    • (2006) J Biol Chem , vol.281 , pp. 30503-30511
    • Prickett, T.D.1    Brautigan, D.L.2
  • 30
    • 0035811068 scopus 로고    scopus 로고
    • Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4
    • Liu J, PrickettTD, Elliott E, Meroni G, Brautigan DL. Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4. Proc Natl Acad Sci U S A. 2001;98:6650-6655.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6650-6655
    • Liu, J.1    Prickett, T.D.2    Elliott, E.3    Meroni, G.4    Brautigan, D.L.5
  • 31
    • 2342489456 scopus 로고    scopus 로고
    • elF-4E expression and its role in malignancies and metastases
    • De Benedetti A, Graff JR. elF-4E expression and its role in malignancies and metastases. Oncogene. 2004;23:3189-3199.
    • (2004) Oncogene , vol.23 , pp. 3189-3199
    • De Benedetti, A.1    Graff, J.R.2
  • 32
    • 0033044355 scopus 로고    scopus 로고
    • elF4E expression in tumors: Its possible role in progression of malignancies
    • De Benedetti A, Harris AL. elF4E expression in tumors: its possible role in progression of malignancies. Int J Biochem Cell Biol. 1999;31:59-72.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 59-72
    • De Benedetti, A.1    Harris, A.L.2
  • 33
    • 0344629665 scopus 로고    scopus 로고
    • Aberrant eukaryotic translation initiation factor 4E-dependent mRNAtransport impedes hematopoietic differentiation and contributes to leukemogenesis
    • Topisirovic I, Guzman ML, McConnell MJ, et al. Aberrant eukaryotic translation initiation factor 4E-dependent mRNAtransport impedes hematopoietic differentiation and contributes to leukemogenesis. Mol Cell Biol. 2003;23:8992-9002.
    • (2003) Mol Cell Biol , vol.23 , pp. 8992-9002
    • Topisirovic, I.1    Guzman, M.L.2    McConnell, M.J.3
  • 34
    • 2342564500 scopus 로고    scopus 로고
    • An essential role for protein synthesis in oncogenic cellular transformation
    • Bader AG, Vogt PK. An essential role for protein synthesis in oncogenic cellular transformation. Oncogene. 2004;23:3145-3150.
    • (2004) Oncogene , vol.23 , pp. 3145-3150
    • Bader, A.G.1    Vogt, P.K.2
  • 35
    • 0023494287 scopus 로고    scopus 로고
    • Kowenz E, Leutz A, Doderlein G, Graf T, Beug H. ts-oncogene-transformed erythroleukemic cells: a novel test system for purifying and characterizing avian erythroid growth factors. In: Neth R, Gallo RC, Greaves MR Kabisch H, eds. Modern Trends in Human Leukemia VII. 31. Heidelberg, Germany: Springer Verlag;1987:199-209.
    • Kowenz E, Leutz A, Doderlein G, Graf T, Beug H. ts-oncogene-transformed erythroleukemic cells: a novel test system for purifying and characterizing avian erythroid growth factors. In: Neth R, Gallo RC, Greaves MR Kabisch H, eds. Modern Trends in Human Leukemia VII. Vol. 31. Heidelberg, Germany: Springer Verlag;1987:199-209.
  • 36
    • 0020122097 scopus 로고
    • Hormone-dependent terminal differentiation in vitro of chicken erythroleukemia cells transformed by ts mutants of avian erythroblastosis virus
    • Beug H, Palmieri S, Freudenstein C, Zentgraf H. Graf T. Hormone-dependent terminal differentiation in vitro of chicken erythroleukemia cells transformed by ts mutants of avian erythroblastosis virus. Cell. 1982;28:907-919.
    • (1982) Cell , vol.28 , pp. 907-919
    • Beug, H.1    Palmieri, S.2    Freudenstein, C.3    Zentgraf, H.4    Graf, T.5
  • 38
    • 0034669936 scopus 로고    scopus 로고
    • Stem cell factor induces phosphatidylinositol 3'-kinasedependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells
    • van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Lowenberg B, von Lindern M. Stem cell factor induces phosphatidylinositol 3'-kinasedependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells. Blood. 2000;96:3406-3413.
    • (2000) Blood , vol.96 , pp. 3406-3413
    • van Dijk, T.B.1    van Den Akker, E.2    Amelsvoort, M.P.3    Mano, H.4    Lowenberg, B.5    von Lindern, M.6
  • 39
    • 4644323788 scopus 로고    scopus 로고
    • Translational control of putative protooncogene Nm23-M2 by cytokines via phosphoinositide 3-kinase signaling
    • Joosten M, Blazquez-Domingo M, Lindeboom F, et al. Translational control of putative protooncogene Nm23-M2 by cytokines via phosphoinositide 3-kinase signaling. J Biol Chem. 2004:279: 38169-38176.
    • (2004) J Biol Chem , vol.279 , pp. 38169-38176
    • Joosten, M.1    Blazquez-Domingo, M.2    Lindeboom, F.3
  • 40
    • 0142152453 scopus 로고    scopus 로고
    • Cooperative signaling between cytokine receptors and the glucocorticoid receptor in the expansion of erythroid progenitors: Molecular analysis by expression profiling
    • Kolbus A, Blazquez-Domingo M, Carotta S, et al. Cooperative signaling between cytokine receptors and the glucocorticoid receptor in the expansion of erythroid progenitors: molecular analysis by expression profiling. Blood. 2003;102:3136-3146.
    • (2003) Blood , vol.102 , pp. 3136-3146
    • Kolbus, A.1    Blazquez-Domingo, M.2    Carotta, S.3
  • 41
    • 12144288611 scopus 로고    scopus 로고
    • Btk is required for an efficient response to erythropoietin and for SCF-controlled protection against TRAIL in erythroid progenitors
    • Schmidt U, van den Akker E, Parren-van Amelsvoort M, et al. Btk is required for an efficient response to erythropoietin and for SCF-controlled protection against TRAIL in erythroid progenitors. J Exp Med. 2004;199:785-795.
    • (2004) J Exp Med , vol.199 , pp. 785-795
    • Schmidt, U.1    van den Akker, E.2    Parren-van Amelsvoort, M.3
  • 42
    • 0038724274 scopus 로고    scopus 로고
    • Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways
    • Matsuda A, Suzuki Y, Honda G, et al. Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003;22:3307-3318.
    • (2003) Oncogene , vol.22 , pp. 3307-3318
    • Matsuda, A.1    Suzuki, Y.2    Honda, G.3
  • 43
    • 33645218017 scopus 로고    scopus 로고
    • Involvement of a novel Q-SNARE, D12, in quality control of the endomembrane system
    • OkumuraA J, Hatsuzawa K, Tamura T, et al. Involvement of a novel Q-SNARE, D12, in quality control of the endomembrane system. J Biol Chem. 2006;281:4495-4506.
    • (2006) J Biol Chem , vol.281 , pp. 4495-4506
    • OkumuraA, J.1    Hatsuzawa, K.2    Tamura, T.3
  • 44
    • 33747876154 scopus 로고    scopus 로고
    • Prolactin activates mammalian target-ofrapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells
    • Bishop JD, Nien WL, Dauphinee SM, Too CK. Prolactin activates mammalian target-ofrapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells. J Endocrinol. 2006;190:307-312.
    • (2006) J Endocrinol , vol.190 , pp. 307-312
    • Bishop, J.D.1    Nien, W.L.2    Dauphinee, S.M.3    Too, C.K.4
  • 45
    • 0033551234 scopus 로고    scopus 로고
    • Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein
    • Peterson RT, Desai BN, Hardwick JS, Schreiber SL. Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein. Proc Natl Acad Sci U S A. 1999;96:4438-4442.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 4438-4442
    • Peterson, R.T.1    Desai, B.N.2    Hardwick, J.S.3    Schreiber, S.L.4
  • 47
    • 0037151120 scopus 로고    scopus 로고
    • Global and specific translational control by rapamycin in T cells uncovered by microarrays and proteomics
    • Grolleau A, Bowman J, Pradet-Balade B, et al. Global and specific translational control by rapamycin in T cells uncovered by microarrays and proteomics. J Biol Chem. 2002;277:22175-22184.
    • (2002) J Biol Chem , vol.277 , pp. 22175-22184
    • Grolleau, A.1    Bowman, J.2    Pradet-Balade, B.3
  • 48
    • 0242361561 scopus 로고    scopus 로고
    • Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes
    • Rajasekhar VK, Viale A, Socci ND, Wiedmann M, Hu X, Holland EC. Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes. Mol Cell. 2003;12:889-901.
    • (2003) Mol Cell , vol.12 , pp. 889-901
    • Rajasekhar, V.K.1    Viale, A.2    Socci, N.D.3    Wiedmann, M.4    Hu, X.5    Holland, E.C.6
  • 49
    • 34250755685 scopus 로고    scopus 로고
    • Epigenetic activation of a subset of mRNAs by elF4E explains its effects on cell proliferation
    • Mamane Y, Petroulakis E, Martineau Y, et al. Epigenetic activation of a subset of mRNAs by elF4E explains its effects on cell proliferation. PLoS ONE. 2007;2:e242.
    • (2007) PLoS ONE , vol.2
    • Mamane, Y.1    Petroulakis, E.2    Martineau, Y.3
  • 50
    • 34547114029 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E induced progression of primary human mammary epithelial cells along the cancer pathway is associated with targeted translational deregulation of oncogenic drivers and inhibitors
    • Larsson O, Li S, Issaenko OA, et al. Eukaryotic translation initiation factor 4E induced progression of primary human mammary epithelial cells along the cancer pathway is associated with targeted translational deregulation of oncogenic drivers and inhibitors. Cancer Res. 2007;67: 6814-6824.
    • (2007) Cancer Res , vol.67 , pp. 6814-6824
    • Larsson, O.1    Li, S.2    Issaenko, O.A.3
  • 51
    • 33748168727 scopus 로고    scopus 로고
    • ILEI: A cytokine essential for EMT tumor formation, and late events in metastasis in epithelial cells
    • Waerner T, Alacakaptan M, Tamir I, et al. ILEI: a cytokine essential for EMT tumor formation, and late events in metastasis in epithelial cells. Cancer Cell. 2006;10:227-239.
    • (2006) Cancer Cell , vol.10 , pp. 227-239
    • Waerner, T.1    Alacakaptan, M.2    Tamir, I.3
  • 52
    • 33745627305 scopus 로고    scopus 로고
    • Global alterations in mRNA polysomal recruitment in a cell model of colorectal cancer progression to metastasis
    • Provenzani A, Fronza R, Loreni F, Pascale A, Amadio M, Quattrone A. Global alterations in mRNA polysomal recruitment in a cell model of colorectal cancer progression to metastasis. Carcinogenesis. 2006;27:1323-1333.
    • (2006) Carcinogenesis , vol.27 , pp. 1323-1333
    • Provenzani, A.1    Fronza, R.2    Loreni, F.3    Pascale, A.4    Amadio, M.5    Quattrone, A.6
  • 53
    • 0026323221 scopus 로고
    • Oligopyrimidine tract at the 5'end of mammalian ribosomal protein mRNAs is required for their translational control
    • Levy S. Avni D, Hariharan N. Perry RP. Meyuhas O. Oligopyrimidine tract at the 5'end of mammalian ribosomal protein mRNAs is required for their translational control. Proc Natl Acad Sci U S A. 1991;88:3319-3323.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3319-3323
    • Levy, S.1    Avni, D.2    Hariharan, N.3    Perry, R.P.4    Meyuhas, O.5
  • 54
    • 0032878232 scopus 로고    scopus 로고
    • Ironregulatory proteins, iron-responsive elements and ferritin mRNA translation
    • Thomson AM, Rogers JT, Leedman PJ. Ironregulatory proteins, iron-responsive elements and ferritin mRNA translation. Int J Biochem Cell Biol. 1999;31:1139-1152.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1139-1152
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 55
    • 17444384228 scopus 로고    scopus 로고
    • Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes
    • Darnell JC, Fraser CE, Mostovetsky O, et al. Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes. Genes Dev. 2005;19:903-918.
    • (2005) Genes Dev , vol.19 , pp. 903-918
    • Darnell, J.C.1    Fraser, C.E.2    Mostovetsky, O.3
  • 56
    • 0033588103 scopus 로고    scopus 로고
    • Translational control by an upstream open reading frame in the HER-2/neu transcript
    • Child SJ, Miller MK, Geballe AP. Translational control by an upstream open reading frame in the HER-2/neu transcript. J Biol Chem. 1999;274: 24335-24341.
    • (1999) J Biol Chem , vol.274 , pp. 24335-24341
    • Child, S.J.1    Miller, M.K.2    Geballe, A.P.3
  • 57
    • 0023425901 scopus 로고
    • Effects of intercistronic length on the efficiency of reinitiation by eucaryotic ribosomes
    • Kozak M. Effects of intercistronic length on the efficiency of reinitiation by eucaryotic ribosomes. Mol Cell Biol. 1987;7:3438-3445.
    • (1987) Mol Cell Biol , vol.7 , pp. 3438-3445
    • Kozak, M.1
  • 58
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and elF-4E BP1 through a common effector mechanism
    • Hara K, Yonezawa K, Weng Q-P, Kozlowski MT, Belham C, Avruch J. Amino acid sufficiency and mTOR regulate p70 S6 kinase and elF-4E BP1 through a common effector mechanism. J Biol Chem. 1998;273:14484-14494.
    • (1998) J Biol Chem , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.-P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 59
    • 0030866101 scopus 로고    scopus 로고
    • PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation
    • Lawrence JC Jr, Fadden P. Haystead TA, Lin TA. PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation. Adv Enzyme Regul. 1997;37:239-267.
    • (1997) Adv Enzyme Regul , vol.37 , pp. 239-267
    • Lawrence Jr, J.C.1    Fadden, P.2    Haystead, T.A.3    Lin, T.A.4
  • 60
    • 12444268260 scopus 로고    scopus 로고
    • Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2Afamily (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein
    • Kloeker S, Reed R, McConnell JL, et al. Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2Afamily (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein. Protein Expr Purif. 2003;31:19-33.
    • (2003) Protein Expr Purif , vol.31 , pp. 19-33
    • Kloeker, S.1    Reed, R.2    McConnell, J.L.3
  • 61
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The Trojan Horse of cellular signaling
    • Sontag E. Protein phosphatase 2A: the Trojan Horse of cellular signaling. Cell Signal. 2001;13: 7-16.
    • (2001) Cell Signal , vol.13 , pp. 7-16
    • Sontag, E.1
  • 62
    • 34247638509 scopus 로고    scopus 로고
    • Subunit composition and developmental regulation of hepatic protein phosphatase 2A(PP2A)
    • Yoo SJ, Boylan JM, Brautigan DL, Gruppuso PA. Subunit composition and developmental regulation of hepatic protein phosphatase 2A(PP2A). Arch Biochem Biophys. 2007;461:186-193.
    • (2007) Arch Biochem Biophys , vol.461 , pp. 186-193
    • Yoo, S.J.1    Boylan, J.M.2    Brautigan, D.L.3    Gruppuso, P.A.4
  • 63
    • 0028021165 scopus 로고
    • Comparison of heterotrimeric protein phosphatase 2A containing different Bsubunits
    • Kamibayashi C, Estes R, Lickteig RL, Yang SI, Craft C, Mumby MC. Comparison of heterotrimeric protein phosphatase 2A containing different Bsubunits. J Biol Chem. 1994;269:20139-20148.
    • (1994) J Biol Chem , vol.269 , pp. 20139-20148
    • Kamibayashi, C.1    Estes, R.2    Lickteig, R.L.3    Yang, S.I.4    Craft, C.5    Mumby, M.C.6
  • 64
    • 0034671578 scopus 로고    scopus 로고
    • TGF-beta inhibits p70 S6 kinase via protein phosphatase 2A to induce G1 arrest
    • Petritsch C, Beug H, Balmain A, Oft M. TGF-beta inhibits p70 S6 kinase via protein phosphatase 2A to induce G1 arrest. Genes Dev. 2000;14: 3093-3101.
    • (2000) Genes Dev , vol.14 , pp. 3093-3101
    • Petritsch, C.1    Beug, H.2    Balmain, A.3    Oft, M.4
  • 65
    • 0026693436 scopus 로고    scopus 로고
    • von Lindern M, van Baal S, Wiegant J, Raap A, Hagemeijer A, Grosveld G. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene. Mol Cell Biol. 1992;12:3346-3355.
    • von Lindern M, van Baal S, Wiegant J, Raap A, Hagemeijer A, Grosveld G. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene. Mol Cell Biol. 1992;12:3346-3355.
  • 66
    • 27644569730 scopus 로고    scopus 로고
    • The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein
    • Neviani P, Santhanam R, Trotta R, et al. The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein. Cancer Cell. 2005;8:355-368.
    • (2005) Cancer Cell , vol.8 , pp. 355-368
    • Neviani, P.1    Santhanam, R.2    Trotta, R.3
  • 67
    • 14944369327 scopus 로고    scopus 로고
    • An erythroid differentiation- specific splicing switch in protein 4.1 R mediated by the interaction of SF2/ASF with an exonic splicing enhancer
    • Yang G, Huang SC, Wu JY, Benz EJ Jr. An erythroid differentiation- specific splicing switch in protein 4.1 R mediated by the interaction of SF2/ASF with an exonic splicing enhancer. Blood. 2005;105:2146-2153.
    • (2005) Blood , vol.105 , pp. 2146-2153
    • Yang, G.1    Huang, S.C.2    Wu, J.Y.3    Benz Jr., E.J.4
  • 68
    • 18744384006 scopus 로고    scopus 로고
    • Decrease in hnRNP A/B expression during erythropoiesis mediates a pre-mRNA splicing switch
    • Hou VC, Lersch R, Gee SL, et al. Decrease in hnRNP A/B expression during erythropoiesis mediates a pre-mRNA splicing switch. EMBO J. 2002;21:6195-6204.
    • (2002) EMBO J , vol.21 , pp. 6195-6204
    • Hou, V.C.1    Lersch, R.2    Gee, S.L.3
  • 69
    • 0036534129 scopus 로고    scopus 로고
    • Alternative splicing: Multiple control mechanisms and involvement in human disease
    • Caceres JF, Kornblihtt AR. Alternative splicing: multiple control mechanisms and involvement in human disease. Trends Genet. 2002;18:186-193.
    • (2002) Trends Genet , vol.18 , pp. 186-193
    • Caceres, J.F.1    Kornblihtt, A.R.2
  • 70
    • 0030760045 scopus 로고    scopus 로고
    • KIS is a protein kinase with an RNA recognition motif
    • MaucuerA, Ozon S, Manceau V. et al. KIS is a protein kinase with an RNA recognition motif. J Biol Chem. 1997;272:23151-23156.
    • (1997) J Biol Chem , vol.272 , pp. 23151-23156
    • Maucuer, A.1    Ozon, S.2    Manceau, V.3
  • 71
    • 0029058415 scopus 로고
    • cornichon and the EGF receptor signaling process are necessary for both anteriorposterior and dorsal-ventral pattern formation in Drosophila
    • Roth S, Neuman-Silberberg FS, Barcelo G, Schupbach T. cornichon and the EGF receptor signaling process are necessary for both anteriorposterior and dorsal-ventral pattern formation in Drosophila. Cell. 1995;81:967-978.
    • (1995) Cell , vol.81 , pp. 967-978
    • Roth, S.1    Neuman-Silberberg, F.S.2    Barcelo, G.3    Schupbach, T.4
  • 72
    • 33747331667 scopus 로고    scopus 로고
    • mED2: A novel gene involved in mouse embryonic development
    • Duan JZ, Zhang JP, Zhu SX. mED2: a novel gene involved in mouse embryonic development. Yi Chuan Xue Bao. 2006;33:692-701.
    • (2006) Yi Chuan Xue Bao , vol.33 , pp. 692-701
    • Duan, J.Z.1    Zhang, J.P.2    Zhu, S.X.3
  • 73
    • 17944377486 scopus 로고    scopus 로고
    • Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR
    • Neshat MS, Mellinghoff IK, Tran C, et al. Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR. Proc Natl Acad Sci U SA. 2001;98:10314-10319.
    • (2001) Proc Natl Acad Sci U SA , vol.98 , pp. 10314-10319
    • Neshat, M.S.1    Mellinghoff, I.K.2    Tran, C.3
  • 74
    • 0037513474 scopus 로고    scopus 로고
    • Constitutive phosphorylation of Akt/PKB protein in acute myeloid leukemia: Its significance as a prognostic variable
    • Min YH, Eom Jl, Cheong JW, et al. Constitutive phosphorylation of Akt/PKB protein in acute myeloid leukemia: its significance as a prognostic variable. Leukemia. 2003;17:995-997.
    • (2003) Leukemia , vol.17 , pp. 995-997
    • Min, Y.H.1    Eom, J.2    Cheong, J.W.3
  • 75
    • 17144387901 scopus 로고    scopus 로고
    • PI3-kinase/Akt is constitutively active in primary acute myeloid leukaemia cells and regulates survival and chemoresistance via NF-kappaB, Mapkinase and p53 pathways
    • Grandage VL, Gale RE, Linch DC, Khwaja A. PI3-kinase/Akt is constitutively active in primary acute myeloid leukaemia cells and regulates survival and chemoresistance via NF-kappaB, Mapkinase and p53 pathways. Leukemia. 2005;19:586-594.
    • (2005) Leukemia , vol.19 , pp. 586-594
    • Grandage, V.L.1    Gale, R.E.2    Linch, D.C.3    Khwaja, A.4
  • 76
    • 22544444889 scopus 로고    scopus 로고
    • Essential role for the pHOdelta isoform in phosphoinositide 3-kinase activation and cell proliferation in acute myeloid leukemia
    • Sujobert P, Bardet V, Cornillet-Lefebvre P, et al. Essential role for the pHOdelta isoform in phosphoinositide 3-kinase activation and cell proliferation in acute myeloid leukemia. Blood. 2005:106: 1063-1066.
    • (2005) Blood , vol.106 , pp. 1063-1066
    • Sujobert, P.1    Bardet, V.2    Cornillet-Lefebvre, P.3
  • 77
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco I, Sawyers CL. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat Rev Cancer. 2002;2:489-501.
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 78
    • 0142227019 scopus 로고    scopus 로고
    • Targeting the PI3K-Akt pathway in human cancer: Rationale and promise
    • Luo J, Manning BD, Cantley LC. Targeting the PI3K-Akt pathway in human cancer: rationale and promise. Cancer Cell. 2003;4:257-262.
    • (2003) Cancer Cell , vol.4 , pp. 257-262
    • Luo, J.1    Manning, B.D.2    Cantley, L.C.3
  • 79
    • 2342559981 scopus 로고    scopus 로고
    • The TOR pathway: A target for cancer therapy
    • Bjornsti MA, Houghton PJ. The TOR pathway: a target for cancer therapy. Nat Rev Cancer. 2004; 4:335-348.
    • (2004) Nat Rev Cancer , vol.4 , pp. 335-348
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 80
    • 0034722888 scopus 로고    scopus 로고
    • The rapamycinsensitive signal transduction pathway as a target for cancer therapy
    • Hidalgo M, Rowinsky EK. The rapamycinsensitive signal transduction pathway as a target for cancer therapy. Oncogene. 2000;19:6680-6686.
    • (2000) Oncogene , vol.19 , pp. 6680-6686
    • Hidalgo, M.1    Rowinsky, E.K.2
  • 81
    • 0842304369 scopus 로고    scopus 로고
    • Mammalian target of rapamycin inhibition as therapy for hematologic malignancies
    • Panwalkar A, Verstovsek S, Giles FJ. Mammalian target of rapamycin inhibition as therapy for hematologic malignancies. Cancer. 2004:100:657-666.
    • (2004) Cancer , vol.100 , pp. 657-666
    • Panwalkar, A.1    Verstovsek, S.2    Giles, F.J.3


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