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Volumn 70, Issue 19, 2013, Pages 3603-3616

The translational factor eIF3f: The ambivalent eIF3 subunit

Author keywords

Apoptosis; Atrophy; Cancer; eIF3f; Hypertrophy

Indexed keywords

CASPASE 3; CDK11 KINASE; CDK11P110 KINASE; CDK11P46 KINASE; EUKARYOTIC INITIATION FACTOR 3F; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; INITIATION FACTOR 3; MAMMALIAN TARGET OF RAPAMYCIN; MSS4 INHIBITOR; NOTCH1 RECEPTOR; PHOSPHOTRANSFERASE; PROTEIN INHIBITOR; PROTEIN KINASE B; RIBOSOME RNA; RNA 18S; RNA 28S; TRANSCRIPTOME; UNCLASSIFIED DRUG;

EID: 84884349758     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1263-y     Document Type: Review
Times cited : (46)

References (94)
  • 1
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • 20094052 10.1038/nrm2838 1:CAS:528:DC%2BC3cXps1Cnuw%3D%3D
    • Jackson RJ, Hellen CU, Pestova TV (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11(2):113-127
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.2 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 2
    • 0034065158 scopus 로고    scopus 로고
    • The structure and function of initiation factors in eukaryotic protein synthesis
    • 11130464 10.1007/PL00000726 1:CAS:528:DC%2BD3cXjvFWltb0%3D
    • Pestova TV, Hellen CU (2000) The structure and function of initiation factors in eukaryotic protein synthesis. Cell Mol Life Sci 57(4):651-674
    • (2000) Cell Mol Life Sci , vol.57 , Issue.4 , pp. 651-674
    • Pestova, T.V.1    Hellen, C.U.2
  • 3
    • 33748924333 scopus 로고    scopus 로고
    • EIF3: A versatile scaffold for translation initiation complexes
    • 16920360 10.1016/j.tibs.2006.08.005 1:CAS:528:DC%2BD28XhtVagtrrP
    • Hinnebusch AG (2006) eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem Sci 31(10):553-562
    • (2006) Trends Biochem Sci , vol.31 , Issue.10 , pp. 553-562
    • Hinnebusch, A.G.1
  • 4
    • 0031033314 scopus 로고    scopus 로고
    • Conservation and diversity of eukaryotic translation initiation factor eIF3
    • 8995409 10.1074/jbc.272.2.1101 1:CAS:528:DyaK2sXmtFGqug%3D%3D
    • Asano K, Kinzy TG, Merrick WC, Hershey JW (1997) Conservation and diversity of eukaryotic translation initiation factor eIF3. J Biol Chem 272(2):1101-1109
    • (1997) J Biol Chem , vol.272 , Issue.2 , pp. 1101-1109
    • Asano, K.1    Kinzy, T.G.2    Merrick, W.C.3    Hershey, J.W.4
  • 5
    • 0030827905 scopus 로고    scopus 로고
    • Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly
    • 9341143 10.1074/jbc.272.43.27042 1:CAS:528:DyaK2sXmvFyrsbo%3D
    • Asano K, Vornlocher HP, Richter-Cook NJ, Merrick WC, Hinnebusch AG, Hershey JW (1997) Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly. J Biol Chem 272(43):27042-27052
    • (1997) J Biol Chem , vol.272 , Issue.43 , pp. 27042-27052
    • Asano, K.1    Vornlocher, H.P.2    Richter-Cook, N.J.3    Merrick, W.C.4    Hinnebusch, A.G.5    Hershey, J.W.6
  • 6
    • 0030433536 scopus 로고    scopus 로고
    • Conservation and diversity in the structure of translation initiation factor EIF3 from humans and yeast
    • 9150866 10.1016/S0300-9084(97)86711-9 1:CAS:528:DyaK2sXjt1Sisbo%3D
    • Hershey JW, Asano K, Naranda T, Vornlocher HP, Hanachi P, Merrick WC (1996) Conservation and diversity in the structure of translation initiation factor EIF3 from humans and yeast. Biochimie 78(11-12):903-907
    • (1996) Biochimie , vol.78 , Issue.11-12 , pp. 903-907
    • Hershey, J.W.1    Asano, K.2    Naranda, T.3    Vornlocher, H.P.4    Hanachi, P.5    Merrick, W.C.6
  • 8
    • 0142057156 scopus 로고    scopus 로고
    • Characterization of eIF3 k: A newly discovered subunit of mammalian translation initiation factor elF3
    • 10.1046/j.1432-1033.2003.03807.x 1:CAS:528:DC%2BD3sXotlGqt74%3D
    • Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (2003) Characterization of eIF3 k: a newly discovered subunit of mammalian translation initiation factor elF3. Eur J Biochem/FEBS 270(20):4133-4139
    • (2003) Eur J Biochem/FEBS , vol.270 , Issue.20 , pp. 4133-4139
    • Mayeur, G.L.1    Fraser, C.S.2    Peiretti, F.3    Block, K.L.4    Hershey, J.W.5
  • 9
    • 0035824649 scopus 로고    scopus 로고
    • The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3
    • 10.1074/jbc.M104966200 11590142 10.1074/jbc.M104966200 1:CAS:528:DC%2BD3MXptVymsLg%3D
    • Morris-Desbois C, Rety S, Ferro M, Garin J, Jalinot P (2001) The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3. J Biol Chem 276(49):45988-45995. doi: 10.1074/jbc.M104966200
    • (2001) J Biol Chem , vol.276 , Issue.49 , pp. 45988-45995
    • Morris-Desbois, C.1    Rety, S.2    Ferro, M.3    Garin, J.4    Jalinot, P.5
  • 10
    • 34250378852 scopus 로고    scopus 로고
    • Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry
    • 10.1074/mcp.M600399-MCP200 17322308 10.1074/mcp.M600399-MCP200 1:CAS:528:DC%2BD2sXnvFyju7w%3D
    • Damoc E, Fraser CS, Zhou M, Videler H, Mayeur GL, Hershey JW, Doudna JA, Robinson CV, Leary JA (2007) Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry. Mol Cell Proteomics 6(7):1135-1146. doi: 10.1074/mcp.M600399-MCP200
    • (2007) Mol Cell Proteomics , vol.6 , Issue.7 , pp. 1135-1146
    • Damoc, E.1    Fraser, C.S.2    Zhou, M.3    Videler, H.4    Mayeur, G.L.5    Hershey, J.W.6    Doudna, J.A.7    Robinson, C.V.8    Leary, J.A.9
  • 12
    • 0017100264 scopus 로고
    • Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes
    • 10.1073/pnas.73.9.3005 1:CAS:528:DyaE28XlsFGgt78%3D
    • Benne R, Hershey JW (1976) Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes. Proc Natll Acad Sci USA 73(9):3005-3009
    • (1976) Proc Natll Acad Sci USA , vol.73 , Issue.9 , pp. 3005-3009
    • Benne, R.1    Hershey, J.W.2
  • 13
    • 0020494571 scopus 로고
    • Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: Comparison of protein structure, activities, and immunochemical properties
    • 6181805 10.1021/bi00261a002 1:CAS:528:DyaL38XltVGksbs%3D
    • Brown-Luedi ML, Meyer LJ, Milburn SC, Yau PM, Corbett S, Hershey JW (1982) Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: comparison of protein structure, activities, and immunochemical properties. Biochemistry 21(18):4202-4206
    • (1982) Biochemistry , vol.21 , Issue.18 , pp. 4202-4206
    • Brown-Luedi, M.L.1    Meyer, L.J.2    Milburn, S.C.3    Yau, P.M.4    Corbett, S.5    Hershey, J.W.6
  • 14
    • 0032541138 scopus 로고    scopus 로고
    • Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae
    • 9660829 10.1074/jbc.273.29.18573 1:CAS:528:DyaK1cXkvVCgtLg%3D
    • Asano K, Phan L, Anderson J, Hinnebusch AG (1998) Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J Biol Chem 273(29):18573-18585
    • (1998) J Biol Chem , vol.273 , Issue.29 , pp. 18573-18585
    • Asano, K.1    Phan, L.2    Anderson, J.3    Hinnebusch, A.G.4
  • 15
    • 0031876171 scopus 로고    scopus 로고
    • Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
    • 9671501 1:CAS:528:DyaK1cXkvVarur4%3D
    • Phan L, Zhang X, Asano K, Anderson J, Vornlocher HP, Greenberg JR, Qin J, Hinnebusch AG (1998) Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol Cell Biol 18(8):4935-4946
    • (1998) Mol Cell Biol , vol.18 , Issue.8 , pp. 4935-4946
    • Phan, L.1    Zhang, X.2    Asano, K.3    Anderson, J.4    Vornlocher, H.P.5    Greenberg, J.R.6    Qin, J.7    Hinnebusch, A.G.8
  • 16
    • 0033610845 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3
    • 9822659 10.1074/jbc.273.48.31901 1:CAS:528:DyaK1cXnvVeltrw%3D
    • Block KL, Vornlocher HP, Hershey JW (1998) Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3. J Biol Chem 273(48):31901-31908
    • (1998) J Biol Chem , vol.273 , Issue.48 , pp. 31901-31908
    • Block, K.L.1    Vornlocher, H.P.2    Hershey, J.W.3
  • 17
    • 0035865256 scopus 로고    scopus 로고
    • Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding
    • 10.1093/emboj/20.4.891 11179233 10.1093/emboj/20.4.891 1:CAS:528:DC%2BD3MXhsVyhtbo%3D
    • Valasek L, Phan L, Schoenfeld LW, Valaskova V, Hinnebusch AG (2001) Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding. EMBO J 20(4):891-904. doi: 10.1093/emboj/20.4.891
    • (2001) EMBO J , vol.20 , Issue.4 , pp. 891-904
    • Valasek, L.1    Phan, L.2    Schoenfeld, L.W.3    Valaskova, V.4    Hinnebusch, A.G.5
  • 18
    • 33645841066 scopus 로고    scopus 로고
    • Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast
    • 10.1128/mcb.26.8.2984-2998.2006 16581774 10.1128/MCB.26.8.2984-2998.2006 1:CAS:528:DC%2BD28Xjs1Sltr8%3D
    • Nielsen KH, Valasek L, Sykes C, Jivotovskaya A, Hinnebusch AG (2006) Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast. Mol Cell Biol 26(8):2984-2998. doi: 10.1128/mcb.26.8.2984-2998.2006
    • (2006) Mol Cell Biol , vol.26 , Issue.8 , pp. 2984-2998
    • Nielsen, K.H.1    Valasek, L.2    Sykes, C.3    Jivotovskaya, A.4    Hinnebusch, A.G.5
  • 19
    • 0035900747 scopus 로고    scopus 로고
    • Dual function of eIF3j/Hcr1p in processing 20 S pre-rRNA and translation initiation
    • 10.1074/jbc.M106887200 11560931 10.1074/jbc.M106887200 1:CAS:528:DC%2BD3MXptleltbw%3D
    • Valasek L, Hasek J, Nielsen KH, Hinnebusch AG (2001) Dual function of eIF3j/Hcr1p in processing 20 S pre-rRNA and translation initiation. J Biol Chem 276(46):43351-43360. doi: 10.1074/jbc.M106887200
    • (2001) J Biol Chem , vol.276 , Issue.46 , pp. 43351-43360
    • Valasek, L.1    Hasek, J.2    Nielsen, K.H.3    Hinnebusch, A.G.4
  • 20
    • 0030832613 scopus 로고    scopus 로고
    • Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation
    • 10.1093/emboj/16.22.6812 9362495 10.1093/emboj/16.22.6812 1:CAS:528:DyaK1cXisVWltA%3D%3D
    • Verlhac MH, Chen RH, Hanachi P, Hershey JW, Derynck R (1997) Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation. EMBO J 16(22):6812-6822. doi: 10.1093/emboj/16.22.6812
    • (1997) EMBO J , vol.16 , Issue.22 , pp. 6812-6822
    • Verlhac, M.H.1    Chen, R.H.2    Hanachi, P.3    Hershey, J.W.4    Derynck, R.5
  • 21
    • 0028568642 scopus 로고
    • Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein
    • 7798228 1:CAS:528:DyaK2cXmvFGmsr0%3D
    • Naranda T, MacMillan SE, Hershey JW (1994) Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein. J Biol Chem 269(51):32286-32292
    • (1994) J Biol Chem , vol.269 , Issue.51 , pp. 32286-32292
    • Naranda, T.1    Macmillan, S.E.2    Hershey, J.W.3
  • 22
    • 0029085423 scopus 로고
    • GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3
    • 7542616 10.1101/gad.9.14.1781 1:CAS:528:DyaK2MXnt1SksLk%3D
    • Garcia-Barrio MT, Naranda T, Vazquez de Aldana CR, Cuesta R, Hinnebusch AG, Hershey JW, Tamame M (1995) GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3. Genes Dev 9(14):1781-1796
    • (1995) Genes Dev , vol.9 , Issue.14 , pp. 1781-1796
    • Garcia-Barrio, M.T.1    Naranda, T.2    Vazquez De Aldana, C.R.3    Cuesta, R.4    Hinnebusch, A.G.5    Hershey, J.W.6    Tamame, M.7
  • 23
    • 0030002818 scopus 로고    scopus 로고
    • SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae
    • 8628297 1:CAS:528:DyaK28XisFektrY%3D
    • Naranda T, MacMillan SE, Donahue TF, Hershey JW (1996) SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol Cell Biol 16(5):2307-2313
    • (1996) Mol Cell Biol , vol.16 , Issue.5 , pp. 2307-2313
    • Naranda, T.1    Macmillan, S.E.2    Donahue, T.F.3    Hershey, J.W.4
  • 24
    • 0032516908 scopus 로고    scopus 로고
    • Rpg1, the Saccharomyces cerevisiae homologue of the largest subunit of mammalian translation initiation factor 3, is required for translational activity
    • 9694884 10.1074/jbc.273.33.21253 1:CAS:528:DyaK1cXlsFOrt74%3D
    • Valasek L, Trachsel H, Hasek J, Ruis H (1998) Rpg1, the Saccharomyces cerevisiae homologue of the largest subunit of mammalian translation initiation factor 3, is required for translational activity. J Biol Chem 273(33):21253-21260
    • (1998) J Biol Chem , vol.273 , Issue.33 , pp. 21253-21260
    • Valasek, L.1    Trachsel, H.2    Hasek, J.3    Ruis, H.4
  • 25
    • 0033546406 scopus 로고    scopus 로고
    • A 110-kilodalton subunit of translation initiation factor eIF3 and an associated 135-kilodalton protein are encoded by the Saccharomyces cerevisiae TIF32 and TIF31 genes
    • 10358023 10.1074/jbc.274.24.16802 1:CAS:528:DyaK1MXjvVGktrw%3D
    • Vornlocher HP, Hanachi P, Ribeiro S, Hershey JW (1999) A 110-kilodalton subunit of translation initiation factor eIF3 and an associated 135-kilodalton protein are encoded by the Saccharomyces cerevisiae TIF32 and TIF31 genes. J Biol Chem 274(24):16802-16812
    • (1999) J Biol Chem , vol.274 , Issue.24 , pp. 16802-16812
    • Vornlocher, H.P.1    Hanachi, P.2    Ribeiro, S.3    Hershey, J.W.4
  • 26
    • 0028947302 scopus 로고
    • Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae
    • 7876188 10.1074/jbc.270.9.4288 1:CAS:528:DyaK2MXktFSitb4%3D
    • Danaie P, Wittmer B, Altmann M, Trachsel H (1995) Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae. J Biol Chem 270(9):4288-4292
    • (1995) J Biol Chem , vol.270 , Issue.9 , pp. 4288-4292
    • Danaie, P.1    Wittmer, B.2    Altmann, M.3    Trachsel, H.4
  • 27
    • 0032483390 scopus 로고    scopus 로고
    • Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic initiation factor 3 and is required for efficient translation initiation
    • 9722586 10.1074/jbc.273.36.23485 1:CAS:528:DyaK1cXlvFakt7g%3D
    • Greenberg JR, Phan L, Gu Z, deSilva A, Apolito C, Sherman F, Hinnebusch AG, Goldfarb DS (1998) Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic initiation factor 3 and is required for efficient translation initiation. J Biol Chem 273(36):23485-23494
    • (1998) J Biol Chem , vol.273 , Issue.36 , pp. 23485-23494
    • Greenberg, J.R.1    Phan, L.2    Gu, Z.3    Desilva, A.4    Apolito, C.5    Sherman, F.6    Hinnebusch, A.G.7    Goldfarb, D.S.8
  • 28
    • 0033605753 scopus 로고    scopus 로고
    • Characterization of the p33 subunit of eukaryotic translation initiation factor-3 from Saccharomyces cerevisiae
    • 10085088 10.1074/jbc.274.13.8546 1:CAS:528:DyaK1MXitFyrsLs%3D
    • Hanachi P, Hershey JW, Vornlocher HP (1999) Characterization of the p33 subunit of eukaryotic translation initiation factor-3 from Saccharomyces cerevisiae. J Biol Chem 274(13):8546-8553
    • (1999) J Biol Chem , vol.274 , Issue.13 , pp. 8546-8553
    • Hanachi, P.1    Hershey, J.W.2    Vornlocher, H.P.3
  • 29
    • 0031023534 scopus 로고    scopus 로고
    • The 39-kilodalton subunit of eukaryotic translation initiation factor 3 is essential for the complex's integrity and for cell viability in Saccharomyces cerevisiae
    • 8972194 1:CAS:528:DyaK2sXhtlWhug%3D%3D
    • Naranda T, Kainuma M, MacMillan SE, Hershey JW (1997) The 39-kilodalton subunit of eukaryotic translation initiation factor 3 is essential for the complex's integrity and for cell viability in Saccharomyces cerevisiae. Mol Cell Biol 17(1):145-153
    • (1997) Mol Cell Biol , vol.17 , Issue.1 , pp. 145-153
    • Naranda, T.1    Kainuma, M.2    Macmillan, S.E.3    Hershey, J.W.4
  • 30
    • 34547178178 scopus 로고    scopus 로고
    • Reconstitution reveals the functional core of mammalian eIF3
    • 10.1038/sj.emboj.7601765 17581632 10.1038/sj.emboj.7601765 1:CAS:528:DC%2BD2sXotFais78%3D
    • Masutani M, Sonenberg N, Yokoyama S, Imataka H (2007) Reconstitution reveals the functional core of mammalian eIF3. EMBO J 26(14):3373-3383. doi: 10.1038/sj.emboj.7601765
    • (2007) EMBO J , vol.26 , Issue.14 , pp. 3373-3383
    • Masutani, M.1    Sonenberg, N.2    Yokoyama, S.3    Imataka, H.4
  • 31
    • 0035253411 scopus 로고    scopus 로고
    • Cell-cycle-dependent translational control
    • 11163145 10.1016/S0959-437X(00)00150-7 1:CAS:528:DC%2BD3MXhtFSnt7w%3D
    • Pyronnet S, Sonenberg N (2001) Cell-cycle-dependent translational control. Curr Opin Genet Dev 11(1):13-18
    • (2001) Curr Opin Genet Dev , vol.11 , Issue.1 , pp. 13-18
    • Pyronnet, S.1    Sonenberg, N.2
  • 32
    • 0031912226 scopus 로고    scopus 로고
    • RPG1: An essential gene of saccharomyces cerevisiae encoding a 110-kDa protein required for passage through the G1 phase
    • 9506897 10.1007/s002940050314 1:CAS:528:DyaK1cXhsFWjs7g%3D
    • Kovarik P, Hasek J, Valasek L, Ruis H (1998) RPG1: an essential gene of saccharomyces cerevisiae encoding a 110-kDa protein required for passage through the G1 phase. Curr Genet 33(2):100-109
    • (1998) Curr Genet , vol.33 , Issue.2 , pp. 100-109
    • Kovarik, P.1    Hasek, J.2    Valasek, L.3    Ruis, H.4
  • 33
    • 0028063950 scopus 로고
    • Cell-cycle mutations among the collection of Saccharomyces cerevisiae dna mutants
    • 8150258 10.1111/j.1574-6968.1994.tb06693.x 1:CAS:528:DyaK2cXitFagt7s%3D
    • Evans DR, Singer RA, Johnston GC, Wheals AE (1994) Cell-cycle mutations among the collection of Saccharomyces cerevisiae dna mutants. FEMS Microbiol Lett 116(2):147-153
    • (1994) FEMS Microbiol Lett , vol.116 , Issue.2 , pp. 147-153
    • Evans, D.R.1    Singer, R.A.2    Johnston, G.C.3    Wheals, A.E.4
  • 34
    • 67349152700 scopus 로고    scopus 로고
    • Role of eIF3a in regulating cell cycle progression
    • 10.1016/j.yexcr.2009.03.009 19327350 10.1016/j.yexcr.2009.03.009 1:CAS:528:DC%2BD1MXms1OqurY%3D
    • Dong Z, Liu Z, Cui P, Pincheira R, Yang Y, Liu J, Zhang JT (2009) Role of eIF3a in regulating cell cycle progression. Exp Cell Res 315(11):1889-1894. doi: 10.1016/j.yexcr.2009.03.009
    • (2009) Exp Cell Res , vol.315 , Issue.11 , pp. 1889-1894
    • Dong, Z.1    Liu, Z.2    Cui, P.3    Pincheira, R.4    Yang, Y.5    Liu, J.6    Zhang, J.T.7
  • 35
    • 16644374780 scopus 로고    scopus 로고
    • Large subunit of translation initiation factor-3 p170 contains potentially functional nuclear localization signals
    • 10.1023/B:MBIL.0000037010.48936.af 1:STN:280:DC%2BD2cvoslyhsQ%3D%3D
    • Chudinova EM, Ivanov PA, Nadezhdina ES (2004) Large subunit of translation initiation factor-3 p170 contains potentially functional nuclear localization signals. Mol Biol (Mosk) 38(4):684-691
    • (2004) Mol Biol (Mosk) , vol.38 , Issue.4 , pp. 684-691
    • Chudinova, E.M.1    Ivanov, P.A.2    Nadezhdina, E.S.3
  • 36
    • 0032755283 scopus 로고    scopus 로고
    • Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies
    • 10504338 1:CAS:528:DyaK1MXntFOju7g%3D
    • Morris-Desbois C, Bochard V, Reynaud C, Jalinot P (1999) Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies. J Cell Sci 112(Pt 19):3331-3342
    • (1999) J Cell Sci , vol.112 , Issue.PART 19 , pp. 3331-3342
    • Morris-Desbois, C.1    Bochard, V.2    Reynaud, C.3    Jalinot, P.4
  • 37
    • 1842556353 scopus 로고    scopus 로고
    • Cell cycle-related variation in subcellular localization of eIF3e/INT6 in human fibroblasts
    • 15030549 10.1111/j.1365-2184.2004.00305.x 1:CAS:528:DC%2BD2cXjslSiurY%3D
    • Watkins SJ, Norbury CJ (2004) Cell cycle-related variation in subcellular localization of eIF3e/INT6 in human fibroblasts. Cell Prolif 37(2):149-160
    • (2004) Cell Prolif , vol.37 , Issue.2 , pp. 149-160
    • Watkins, S.J.1    Norbury, C.J.2
  • 38
    • 4344624403 scopus 로고    scopus 로고
    • Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3 k) as a new interaction partner of cyclin D3
    • 10.1016/j.febslet.2004.07.071 15327989 10.1016/j.febslet.2004.07.071 1:CAS:528:DC%2BD2cXmvFyrtrc%3D
    • Shen X, Yang Y, Liu W, Sun M, Jiang J, Zong H, Gu J (2004) Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3 k) as a new interaction partner of cyclin D3. FEBS Lett 573(1-3):139-146. doi: 10.1016/j.febslet.2004.07.071
    • (2004) FEBS Lett , vol.573 , Issue.1-3 , pp. 139-146
    • Shen, X.1    Yang, Y.2    Liu, W.3    Sun, M.4    Jiang, J.5    Zong, H.6    Gu, J.7
  • 39
    • 0038136969 scopus 로고    scopus 로고
    • The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47 subunit of eukaryotic initiation factor 3 during apoptosis
    • 12446680 10.1074/jbc.M206427200 1:CAS:528:DC%2BD3sXhtVKlt7w%3D
    • Shi J, Feng Y, Goulet AC, Vaillancourt RR, Sachs NA, Hershey JW, Nelson MA (2003) The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47 subunit of eukaryotic initiation factor 3 during apoptosis. J Biol Chem 278(7):5062-5071
    • (2003) J Biol Chem , vol.278 , Issue.7 , pp. 5062-5071
    • Shi, J.1    Feng, Y.2    Goulet, A.C.3    Vaillancourt, R.R.4    Sachs, N.A.5    Hershey, J.W.6    Nelson, M.A.7
  • 40
    • 78149240561 scopus 로고    scopus 로고
    • Regulation of protein synthesis and the role of eIF3 in cancer
    • 20922269 10.1590/S0100-879X2010007500098 1:CAS:528:DC%2BC3cXhsFyhtr%2FK
    • Hershey JW (2010) Regulation of protein synthesis and the role of eIF3 in cancer. Braz J Med Biol Res 43(10):920-930
    • (2010) Braz J Med Biol Res , vol.43 , Issue.10 , pp. 920-930
    • Hershey, J.W.1
  • 41
    • 77950002202 scopus 로고    scopus 로고
    • Translational control in cancer
    • 20332778 10.1038/nrc2824 1:CAS:528:DC%2BC3cXjslWiu7o%3D
    • Silvera D, Formenti SC, Schneider RJ (2010) Translational control in cancer. Nat Rev Cancer 10(4):254-266
    • (2010) Nat Rev Cancer , vol.10 , Issue.4 , pp. 254-266
    • Silvera, D.1    Formenti, S.C.2    Schneider, R.J.3
  • 42
    • 33748042296 scopus 로고    scopus 로고
    • Initiation factor eIF3 and regulation of mRNA translation, cell growth, and cancer
    • 10.1016/j.critrevonc.2006.03.005 10.1016/j.critrevonc.2006.03.005
    • Dong Z, Zhang JT (2006) Initiation factor eIF3 and regulation of mRNA translation, cell growth, and cancer. Crit Rev Oncol/Hematol 59(3):169-180. doi: 10.1016/j.critrevonc.2006.03.005
    • (2006) Crit Rev Oncol/Hematol , vol.59 , Issue.3 , pp. 169-180
    • Dong, Z.1    Zhang, J.T.2
  • 43
    • 0034671570 scopus 로고    scopus 로고
    • A new pathway of translational regulation mediated by eukaryotic initiation factor 3
    • 10.1093/emboj/19.24.6891 11118224 10.1093/emboj/19.24.6891 1:CAS:528:DC%2BD3MXns1alsg%3D%3D
    • Guo J, Hui DJ, Merrick WC, Sen GC (2000) A new pathway of translational regulation mediated by eukaryotic initiation factor 3. EMBO J 19(24):6891-6899. doi: 10.1093/emboj/19.24.6891
    • (2000) EMBO J , vol.19 , Issue.24 , pp. 6891-6899
    • Guo, J.1    Hui, D.J.2    Merrick, W.C.3    Sen, G.C.4
  • 44
    • 0141891214 scopus 로고    scopus 로고
    • Viral stress-inducible protein p56 inhibits translation by blocking the interaction of eIF3 with the ternary complex eIF2.GTP.Met-tRNAi
    • 10.1074/jbc.M305038200 12885778 10.1074/jbc.M305038200 1:CAS:528:DC%2BD3sXnvFant7s%3D
    • Hui DJ, Bhasker CR, Merrick WC, Sen GC (2003) Viral stress-inducible protein p56 inhibits translation by blocking the interaction of eIF3 with the ternary complex eIF2.GTP.Met-tRNAi. J Biol Chem 278(41):39477-39482. doi: 10.1074/jbc.M305038200
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 39477-39482
    • Hui, D.J.1    Bhasker, C.R.2    Merrick, W.C.3    Sen, G.C.4
  • 45
    • 55449106579 scopus 로고    scopus 로고
    • Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation
    • 10.1128/mcb.00738-08 18725400 10.1128/MCB.00738-08 1:CAS:528: DC%2BD1cXhtlWiu7bF
    • Martineau Y, Derry MC, Wang X, Yanagiya A, Berlanga JJ, Shyu AB, Imataka H, Gehring K, Sonenberg N (2008) Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation. Mol Cell Biol 28(21):6658-6667. doi: 10.1128/mcb.00738-08
    • (2008) Mol Cell Biol , vol.28 , Issue.21 , pp. 6658-6667
    • Martineau, Y.1    Derry, M.C.2    Wang, X.3    Yanagiya, A.4    Berlanga, J.J.5    Shyu, A.B.6    Imataka, H.7    Gehring, K.8    Sonenberg, N.9
  • 46
    • 75149146624 scopus 로고    scopus 로고
    • The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways
    • 10.1158/1541-7786.mcr-08-0491 10.1158/1541-7786.MCR-08-0491 1:CAS:528:DC%2BC3cXntVCgug%3D%3D
    • Lee JP, Brauweiler A, Rudolph M, Hooper JE, Drabkin HA, Gemmill RM (2010) The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways. Mol Cancer Res MCR 8(1):93-106. doi: 10.1158/1541-7786.mcr-08-0491
    • (2010) Mol Cancer Res MCR , vol.8 , Issue.1 , pp. 93-106
    • Lee, J.P.1    Brauweiler, A.2    Rudolph, M.3    Hooper, J.E.4    Drabkin, H.A.5    Gemmill, R.M.6
  • 47
    • 79251623048 scopus 로고    scopus 로고
    • EIF3 m expression influences the regulation of tumorigenesis-related genes in human colon cancer
    • 10.1038/onc.2010.422 20838379 10.1038/onc.2010.422 1:CAS:528: DC%2BC3cXhtFGgtrjO
    • Goh SH, Hong SH, Lee BC, Ju MH, Jeong JS, Cho YR, Kim IH, Lee YS (2011) eIF3 m expression influences the regulation of tumorigenesis-related genes in human colon cancer. Oncogene 30(4):398-409. doi: 10.1038/onc.2010.422
    • (2011) Oncogene , vol.30 , Issue.4 , pp. 398-409
    • Goh, S.H.1    Hong, S.H.2    Lee, B.C.3    Ju, M.H.4    Jeong, J.S.5    Cho, Y.R.6    Kim, I.H.7    Lee, Y.S.8
  • 48
    • 34247165835 scopus 로고    scopus 로고
    • Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells
    • 17170115 10.1074/jbc.M606284200 1:CAS:528:DC%2BD2sXhvVaiurs%3D
    • Zhang L, Pan X, Hershey JW (2007) Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells. J Biol Chem 282(8):5790-5800
    • (2007) J Biol Chem , vol.282 , Issue.8 , pp. 5790-5800
    • Zhang, L.1    Pan, X.2    Hershey, J.W.3
  • 49
    • 53049108498 scopus 로고    scopus 로고
    • An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3
    • 10.1074/jbc.M800956200 18544531 10.1074/jbc.M800956200 1:CAS:528:DC%2BD1cXhtVWktrvN
    • Zhang L, Smit-McBride Z, Pan X, Rheinhardt J, Hershey JW (2008) An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3. J Biol Chem 283(35):24047-24060. doi: 10.1074/jbc.M800956200
    • (2008) J Biol Chem , vol.283 , Issue.35 , pp. 24047-24060
    • Zhang, L.1    Smit-Mcbride, Z.2    Pan, X.3    Rheinhardt, J.4    Hershey, J.W.5
  • 50
    • 0031573377 scopus 로고    scopus 로고
    • The chromosome location of the human homolog of the mouse mammary tumor-associated gene INT6 and its status in human breast carcinomas
    • 10.1006/geno.1997.4996 9403073 10.1006/geno.1997.4996 1:CAS:528:DyaK2sXnvVGks74%3D
    • Miyazaki S, Imatani A, Ballard L, Marchetti A, Buttitta F, Albertsen H, Nevanlinna HA, Gallahan D, Callahan R (1997) The chromosome location of the human homolog of the mouse mammary tumor-associated gene INT6 and its status in human breast carcinomas. Genomics 46(1):155-158. doi: 10.1006/geno.1997.4996
    • (1997) Genomics , vol.46 , Issue.1 , pp. 155-158
    • Miyazaki, S.1    Imatani, A.2    Ballard, L.3    Marchetti, A.4    Buttitta, F.5    Albertsen, H.6    Nevanlinna, H.A.7    Gallahan, D.8    Callahan, R.9
  • 51
    • 0035227065 scopus 로고    scopus 로고
    • Reduced expression of INT-6/eIF3-p48 in human tumors
    • 11115556 1:CAS:528:DC%2BD3MXhtlGitw%3D%3D
    • Marchetti A, Buttitta F, Pellegrini S, Bertacca G, Callahan R (2001) Reduced expression of INT-6/eIF3-p48 in human tumors. Int J Oncol 18(1):175-179
    • (2001) Int J Oncol , vol.18 , Issue.1 , pp. 175-179
    • Marchetti, A.1    Buttitta, F.2    Pellegrini, S.3    Bertacca, G.4    Callahan, R.5
  • 55
    • 33746899672 scopus 로고    scopus 로고
    • Decreased expression of eukaryotic initiation factor 3f deregulates translation and apoptosis in tumor cells
    • 16532022 10.1038/sj.onc.1209495 1:CAS:528:DC%2BD28XnvVyltr0%3D
    • Shi J, Kahle A, Hershey JW, Honchak BM, Warneke JA, Leong SP, Nelson MA (2006) Decreased expression of eukaryotic initiation factor 3f deregulates translation and apoptosis in tumor cells. Oncogene 25(35):4923-4936
    • (2006) Oncogene , vol.25 , Issue.35 , pp. 4923-4936
    • Shi, J.1    Kahle, A.2    Hershey, J.W.3    Honchak, B.M.4    Warneke, J.A.5    Leong, S.P.6    Nelson, M.A.7
  • 56
    • 84858767569 scopus 로고    scopus 로고
    • The tumor suppressive role of eIF3f and its function in translation inhibition and rRNA degradation
    • 22457825 10.1371/journal.pone.0034194 1:CAS:528:DC%2BC38XltF2kt7s%3D
    • Wen F, Zhou R, Shen A, Choi A, Uribe D, Shi J (2012) The tumor suppressive role of eIF3f and its function in translation inhibition and rRNA degradation. PLoS ONE 7(3):e34194
    • (2012) PLoS ONE , vol.7 , Issue.3 , pp. 34194
    • Wen, F.1    Zhou, R.2    Shen, A.3    Choi, A.4    Uribe, D.5    Shi, J.6
  • 57
    • 63149126092 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by eIF3f
    • 10.1073/pnas.0900557106 10.1073/pnas.0900557106 1:CAS:528: DC%2BD1MXjslyhs7Y%3D
    • Valente ST, Gilmartin GM, Mott C, Falkard B, Goff SP (2009) Inhibition of HIV-1 replication by eIF3f. Proc Natll Acad Sci USA 106(11):4071-4078. doi: 10.1073/pnas.0900557106
    • (2009) Proc Natll Acad Sci USA , vol.106 , Issue.11 , pp. 4071-4078
    • Valente, S.T.1    Gilmartin, G.M.2    Mott, C.3    Falkard, B.4    Goff, S.P.5
  • 58
    • 70350004235 scopus 로고    scopus 로고
    • HIV-1 mRNA 3′ end processing is distinctively regulated by eIF3f, CDK11, and splice factor 9G8
    • 10.1016/j.molcel.2009.10.004 19854136 10.1016/j.molcel.2009.10.004 1:CAS:528:DC%2BD1MXhsFWht7vP
    • Valente ST, Gilmartin GM, Venkatarama K, Arriagada G, Goff SP (2009) HIV-1 mRNA 3′ end processing is distinctively regulated by eIF3f, CDK11, and splice factor 9G8. Mol Cell 36(2):279-289. doi: 10.1016/j.molcel.2009.10.004
    • (2009) Mol Cell , vol.36 , Issue.2 , pp. 279-289
    • Valente, S.T.1    Gilmartin, G.M.2    Venkatarama, K.3    Arriagada, G.4    Goff, S.P.5
  • 59
    • 0036000003 scopus 로고    scopus 로고
    • Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome
    • 12006658 10.1091/mbc.01-06-0301 1:CAS:528:DC%2BD38XktFyru7c%3D
    • Dunand-Sauthier I, Walker C, Wilkinson C, Gordon C, Crane R, Norbury C, Humphrey T (2002) Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome. Mol Biol Cell 13(5):1626-1640
    • (2002) Mol Biol Cell , vol.13 , Issue.5 , pp. 1626-1640
    • Dunand-Sauthier, I.1    Walker, C.2    Wilkinson, C.3    Gordon, C.4    Crane, R.5    Norbury, C.6    Humphrey, T.7
  • 60
    • 61749091373 scopus 로고    scopus 로고
    • Phosphorylation of the eukaryotic initiation factor 3f by cyclin-dependent kinase 11 during apoptosis
    • 19245811 10.1016/j.febslet.2009.02.028 1:CAS:528:DC%2BD1MXjt1Kmurs%3D
    • Shi J, Hershey JW, Nelson MA (2009) Phosphorylation of the eukaryotic initiation factor 3f by cyclin-dependent kinase 11 during apoptosis. FEBS Lett 583(6):971-977
    • (2009) FEBS Lett , vol.583 , Issue.6 , pp. 971-977
    • Shi, J.1    Hershey, J.W.2    Nelson, M.A.3
  • 61
    • 0031836475 scopus 로고    scopus 로고
    • Homologues of 26S proteasome subunits are regulators of transcription and translation
    • 10.1002/pro.5560070521 9605331 10.1002/pro.5560070521 1:CAS:528:DyaK1cXivFKktbc%3D
    • Aravind L, Ponting CP (1998) Homologues of 26S proteasome subunits are regulators of transcription and translation. Protein Sci 7(5):1250-1254. doi: 10.1002/pro.5560070521
    • (1998) Protein Sci , vol.7 , Issue.5 , pp. 1250-1254
    • Aravind, L.1    Ponting, C.P.2
  • 62
    • 0032104227 scopus 로고    scopus 로고
    • The PCI domain: A common theme in three multiprotein complexes
    • 9644972 10.1016/S0968-0004(98)01217-1 1:CAS:528:DyaK1cXktVSlsLg%3D
    • Hofmann K, Bucher P (1998) The PCI domain: a common theme in three multiprotein complexes. Trends Biochem Sci 23(6):204-205
    • (1998) Trends Biochem Sci , vol.23 , Issue.6 , pp. 204-205
    • Hofmann, K.1    Bucher, P.2
  • 63
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • 10.1093/emboj/20.24.7096 11742986 10.1093/emboj/20.24.7096 1:CAS:528:DC%2BD38XpsFOl
    • Fu H, Reis N, Lee Y, Glickman MH, Vierstra RD (2001) Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J 20(24):7096-7107. doi: 10.1093/emboj/20.24.7096
    • (2001) EMBO J , vol.20 , Issue.24 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.D.5
  • 64
    • 34250187773 scopus 로고    scopus 로고
    • The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer
    • 10.1016/j.jmb.2007.04.084 17559875 10.1016/j.jmb.2007.04.084 1:CAS:528:DC%2BD2sXmsFClu7w%3D
    • Sanches M, Alves BS, Zanchin NI, Guimaraes BG (2007) The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer. J Mol Biol 370(5):846-855. doi: 10.1016/j.jmb.2007.04.084
    • (2007) J Mol Biol , vol.370 , Issue.5 , pp. 846-855
    • Sanches, M.1    Alves, B.S.2    Zanchin, N.I.3    Guimaraes, B.G.4
  • 65
    • 84859897175 scopus 로고    scopus 로고
    • The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6
    • 10.1016/j.febslet.2012.03.029 22575649 10.1016/j.febslet.2012.03.029 1:CAS:528:DC%2BC38XkvFWqt70%3D
    • Zhang H, Gao ZQ, Wang WJ, Liu GF, Shtykova EV, Xu JH, Li LF, Su XD, Dong YH (2012) The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6. FEBS Lett 586(8):1147-1153. doi: 10.1016/j.febslet.2012.03.029
    • (2012) FEBS Lett , vol.586 , Issue.8 , pp. 1147-1153
    • Zhang, H.1    Gao, Z.Q.2    Wang, W.J.3    Liu, G.F.4    Shtykova, E.V.5    Xu, J.H.6    Li, L.F.7    Su, X.D.8    Dong, Y.H.9
  • 66
    • 0025016167 scopus 로고
    • Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle
    • 10.1073/pnas.87.19.7467 1:CAS:528:DyaK3MXnvFamtQ%3D%3D
    • Bunnell BA, Heath LS, Adams DE, Lahti JM, Kidd VJ (1990) Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle. Proc Natll Acad Sci USA 87(19):7467-7471
    • (1990) Proc Natll Acad Sci USA , vol.87 , Issue.19 , pp. 7467-7471
    • Bunnell, B.A.1    Heath, L.S.2    Adams, D.E.3    Lahti, J.M.4    Kidd, V.J.5
  • 67
    • 0031809282 scopus 로고    scopus 로고
    • The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo
    • 9580558 1:CAS:528:DyaK1cXktFCju7Y%3D
    • Loyer P, Trembley JH, Lahti JM, Kidd VJ (1998) The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo. J Cell Sci 111(Pt 11):1495-1506
    • (1998) J Cell Sci , vol.111 , Issue.PART 11 , pp. 1495-1506
    • Loyer, P.1    Trembley, J.H.2    Lahti, J.M.3    Kidd, V.J.4
  • 68
    • 0037067772 scopus 로고    scopus 로고
    • Cyclin L is an RS domain protein involved in pre-mRNA splicing
    • 10.1074/jbc.M202266200 11980906 10.1074/jbc.M202266200 1:CAS:528:DC%2BD38XlsVWhs7c%3D
    • Dickinson LA, Edgar AJ, Ehley J, Gottesfeld JM (2002) Cyclin L is an RS domain protein involved in pre-mRNA splicing. J Biol Chem 277(28):25465-25473. doi: 10.1074/jbc.M202266200
    • (2002) J Biol Chem , vol.277 , Issue.28 , pp. 25465-25473
    • Dickinson, L.A.1    Edgar, A.J.2    Ehley, J.3    Gottesfeld, J.M.4
  • 69
    • 0028335403 scopus 로고
    • Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms
    • 8195233 1:CAS:528:DyaK2cXlt1yltrs%3D
    • Xiang J, Lahti JM, Grenet J, Easton J, Kidd VJ (1994) Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms. J Biol Chem 269(22):15786-15794
    • (1994) J Biol Chem , vol.269 , Issue.22 , pp. 15786-15794
    • Xiang, J.1    Lahti, J.M.2    Grenet, J.3    Easton, J.4    Kidd, V.J.5
  • 70
    • 0033215243 scopus 로고    scopus 로고
    • Fas-induced apoptosis in human malignant melanoma cell lines is associated with the activation of the p34(cdc2)-related PITSLRE protein kinases
    • 10497214 10.1074/jbc.274.40.28505 1:CAS:528:DyaK1MXmsFWgurY%3D
    • Ariza ME, Broome-Powell M, Lahti JM, Kidd VJ, Nelson MA (1999) Fas-induced apoptosis in human malignant melanoma cell lines is associated with the activation of the p34(cdc2)-related PITSLRE protein kinases. J Biol Chem 274(40):28505-28513
    • (1999) J Biol Chem , vol.274 , Issue.40 , pp. 28505-28513
    • Ariza, M.E.1    Broome-Powell, M.2    Lahti, J.M.3    Kidd, V.J.4    Nelson, M.A.5
  • 71
    • 0030973423 scopus 로고    scopus 로고
    • Cleavage of PITSLRE kinases by ICE/CASP-1 and CPP32/CASP-3 during apoptosis induced by tumor necrosis factor
    • 9115219 10.1074/jbc.272.18.11694 1:CAS:528:DyaK2sXivF2ksb8%3D
    • Beyaert R, Kidd VJ, Cornelis S, Van de Craen M, Denecker G, Lahti JM, Gururajan R, Vandenabeele P, Fiers W (1997) Cleavage of PITSLRE kinases by ICE/CASP-1 and CPP32/CASP-3 during apoptosis induced by tumor necrosis factor. J Biol Chem 272(18):11694-11697
    • (1997) J Biol Chem , vol.272 , Issue.18 , pp. 11694-11697
    • Beyaert, R.1    Kidd, V.J.2    Cornelis, S.3    Van De Craen, M.4    Denecker, G.5    Lahti, J.M.6    Gururajan, R.7    Vandenabeele, P.8    Fiers, W.9
  • 72
    • 22344452754 scopus 로고    scopus 로고
    • The binding activity of yeast RNAs to yeast Hek2p and mammalian hnRNP K proteins, determined using the three-hybrid system
    • 16010288 1:CAS:528:DC%2BD2MXnsVCju7o%3D
    • Paziewska A, Wyrwicz LS, Ostrowski J (2005) The binding activity of yeast RNAs to yeast Hek2p and mammalian hnRNP K proteins, determined using the three-hybrid system. Cell Mol Biol Lett 10(2):227-235
    • (2005) Cell Mol Biol Lett , vol.10 , Issue.2 , pp. 227-235
    • Paziewska, A.1    Wyrwicz, L.S.2    Ostrowski, J.3
  • 74
    • 49049083353 scopus 로고    scopus 로고
    • Signaling in muscle atrophy and hypertrophy
    • 10.1152/physiol.00041.2007 18556469 10.1152/physiol.00041.2007 1:CAS:528:DC%2BD1cXosFKhtLY%3D
    • Sandri M (2008) Signaling in muscle atrophy and hypertrophy. Physiology 23:160-170. doi: 10.1152/physiol.00041.2007
    • (2008) Physiology , vol.23 , pp. 160-170
    • Sandri, M.1
  • 75
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • 10.1101/gad.1212704 15314020 10.1101/gad.1212704 1:CAS:528: DC%2BD2cXmvFKqsLk%3D
    • Hay N, Sonenberg N (2004) Upstream and downstream of mTOR. Genes Dev 18(16):1926-1945. doi: 10.1101/gad.1212704
    • (2004) Genes Dev , vol.18 , Issue.16 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 76
    • 37449029143 scopus 로고    scopus 로고
    • Nutritional control of protein biosynthetic capacity by insulin via Myc in Drosophila
    • 10.1016/j.cmet.2007.11.010 18177722 10.1016/j.cmet.2007.11.010 1:CAS:528:DC%2BD1cXnsFSnsw%3D%3D
    • Teleman AA, Hietakangas V, Sayadian AC, Cohen SM (2008) Nutritional control of protein biosynthetic capacity by insulin via Myc in Drosophila. Cell Metab 7(1):21-32. doi: 10.1016/j.cmet.2007.11.010
    • (2008) Cell Metab , vol.7 , Issue.1 , pp. 21-32
    • Teleman, A.A.1    Hietakangas, V.2    Sayadian, A.C.3    Cohen, S.M.4
  • 78
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
    • 10.1073/pnas.142166599 10.1073/pnas.142166599 1:CAS:528: DC%2BD38XlsVGgs7w%3D
    • Pallafacchina G, Calabria E, Serrano AL, Kalhovde JM, Schiaffino S (2002) A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification. Proc Natll Acad Sci USA 99(14):9213-9218. doi: 10.1073/pnas.142166599
    • (2002) Proc Natll Acad Sci USA , vol.99 , Issue.14 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 79
    • 27744569843 scopus 로고    scopus 로고
    • MTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • 10.1016/j.cell.2005.10.024 16286006 10.1016/j.cell.2005.10.024 1:CAS:528:DC%2BD2MXht1yktrvK
    • Holz MK, Ballif BA, Gygi SP, Blenis J (2005) mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123(4):569-580. doi: 10.1016/j.cell.2005.10.024
    • (2005) Cell , vol.123 , Issue.4 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 80
    • 33646124490 scopus 로고    scopus 로고
    • MTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin
    • 10.1038/sj.emboj.7601047 16541103 10.1038/sj.emboj.7601047 1:CAS:528:DC%2BD28XjsFaktr8%3D
    • Harris TE, Chi A, Shabanowitz J, Hunt DF, Rhoads RE, Lawrence JC Jr (2006) mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin. EMBO J 25(8):1659-1668. doi: 10.1038/sj.emboj.7601047
    • (2006) EMBO J , vol.25 , Issue.8 , pp. 1659-1668
    • Harris, T.E.1    Chi, A.2    Shabanowitz, J.3    Hunt, D.F.4    Rhoads, R.E.5    Lawrence, Jr.J.C.6
  • 81
    • 47249141703 scopus 로고    scopus 로고
    • EIF3-f function in skeletal muscles: To stand at the crossroads of atrophy and hypertrophy
    • 18583931 10.4161/cc.7.12.6090 1:CAS:528:DC%2BD1cXhtVehtLjN
    • Csibi A, Tintignac LA, Leibovitch MP, Leibovitch SA (2008) eIF3-f function in skeletal muscles: to stand at the crossroads of atrophy and hypertrophy. Cell Cycle 7(12):1698-1701
    • (2008) Cell Cycle , vol.7 , Issue.12 , pp. 1698-1701
    • Csibi, A.1    Tintignac, L.A.2    Leibovitch, M.P.3    Leibovitch, S.A.4
  • 82
    • 50649084799 scopus 로고    scopus 로고
    • All translation elongation factors and the e, f, and h subunits of translation initiation factor 3 are encoded by 5′-terminal oligopyrimidine (TOP) mRNAs
    • 10.1261/rna.1037108 18658124 10.1261/rna.1037108 1:CAS:528: DC%2BD1cXhtFSnu7vK
    • Iadevaia V, Caldarola S, Tino E, Amaldi F, Loreni F (2008) All translation elongation factors and the e, f, and h subunits of translation initiation factor 3 are encoded by 5′-terminal oligopyrimidine (TOP) mRNAs. RNA 14(9):1730-1736. doi: 10.1261/rna.1037108
    • (2008) RNA , vol.14 , Issue.9 , pp. 1730-1736
    • Iadevaia, V.1    Caldarola, S.2    Tino, E.3    Amaldi, F.4    Loreni, F.5
  • 83
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • 10.1046/j.1432-1327.2000.01719.x 1:CAS:528:DC%2BD3cXnvVGjsrY%3D
    • Meyuhas O (2000) Synthesis of the translational apparatus is regulated at the translational level. Eur J Biochem/FEBS 267(21):6321-6330
    • (2000) Eur J Biochem/FEBS , vol.267 , Issue.21 , pp. 6321-6330
    • Meyuhas, O.1
  • 84
    • 13444252523 scopus 로고    scopus 로고
    • Recent advances in the regulation of the TOR pathway by insulin and nutrients
    • 15586002 10.1097/00075197-200501000-00010 1:CAS:528:DC%2BD2MXhsVyltLg%3D
    • Avruch J, Lin Y, Long X, Murthy S, Ortiz-Vega S (2005) Recent advances in the regulation of the TOR pathway by insulin and nutrients. Curr Opin Clin Nutr Metab Care 8(1):67-72
    • (2005) Curr Opin Clin Nutr Metab Care , vol.8 , Issue.1 , pp. 67-72
    • Avruch, J.1    Lin, Y.2    Long, X.3    Murthy, S.4    Ortiz-Vega, S.5
  • 85
    • 84860527756 scopus 로고    scopus 로고
    • A unifying model for mTORC1-mediated regulation of mRNA translation
    • 10.1038/nature11083 22552098 10.1038/nature11083 1:CAS:528: DC%2BC38XmsFCgtb8%3D
    • Thoreen CC, Chantranupong L, Keys HR, Wang T, Gray NS, Sabatini DM (2012) A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 485(7396):109-113. doi: 10.1038/nature11083
    • (2012) Nature , vol.485 , Issue.7396 , pp. 109-113
    • Thoreen, C.C.1    Chantranupong, L.2    Keys, H.R.3    Wang, T.4    Gray, N.S.5    Sabatini, D.M.6
  • 86
    • 77749299092 scopus 로고    scopus 로고
    • The translation regulatory subunit eIF3f controls the kinase-dependent mTOR signaling required for muscle differentiation and hypertrophy in mouse
    • 10.1371/journal.pone.0008994 20126553 10.1371/journal.pone.0008994
    • Csibi A, Cornille K, Leibovitch MP, Poupon A, Tintignac LA, Sanchez AM, Leibovitch SA (2010) The translation regulatory subunit eIF3f controls the kinase-dependent mTOR signaling required for muscle differentiation and hypertrophy in mouse. PLoS ONE 5(2):e8994. doi: 10.1371/journal.pone.0008994
    • (2010) PLoS ONE , vol.5 , Issue.2 , pp. 8994
    • Csibi, A.1    Cornille, K.2    Leibovitch, M.P.3    Poupon, A.4    Tintignac, L.A.5    Sanchez, A.M.6    Leibovitch, S.A.7
  • 87
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • 10.1073/pnas.251541198 11717410 10.1073/pnas.251541198 1:CAS:528:DC%2BD3MXptFCltbs%3D
    • Gomes MD, Lecker SH, Jagoe RT, Navon A, Goldberg AL (2001) Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci USA 98(25):14440-14445. doi: 10.1073/pnas.251541198
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.25 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 89
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • 10.1096/fj.06-6604com 17116744 10.1096/fj.06-6604com 1:CAS:528: DC%2BD2sXmvFCjug%3D%3D
    • Sacheck JM, Hyatt JP, Raffaello A, Jagoe RT, Roy RR, Edgerton VR, Lecker SH, Goldberg AL (2007) Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases. FASEB J 21(1):140-155. doi: 10.1096/fj.06-6604com
    • (2007) FASEB J , vol.21 , Issue.1 , pp. 140-155
    • Sacheck, J.M.1    Hyatt, J.P.2    Raffaello, A.3    Jagoe, R.T.4    Roy, R.R.5    Edgerton, V.R.6    Lecker, S.H.7    Goldberg, A.L.8
  • 90
    • 63249134179 scopus 로고    scopus 로고
    • MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines
    • 10.1074/jbc.M807641200 19073596 10.1074/jbc.M807641200 1:CAS:528:DC%2BD1MXhsFOjsrw%3D
    • Csibi A, Leibovitch MP, Cornille K, Tintignac LA, Leibovitch SA (2009) MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines. J Biol Chem 284(7):4413-4421. doi: 10.1074/jbc.M807641200
    • (2009) J Biol Chem , vol.284 , Issue.7 , pp. 4413-4421
    • Csibi, A.1    Leibovitch, M.P.2    Cornille, K.3    Tintignac, L.A.4    Leibovitch, S.A.5
  • 91
    • 42449129752 scopus 로고    scopus 로고
    • The initiation factor eIF3-f is a major target for atrogin1/MAFbx function in skeletal muscle atrophy
    • 10.1038/emboj.2008.52 18354498 10.1038/emboj.2008.52 1:CAS:528: DC%2BD1cXkvFyltLc%3D
    • Lagirand-Cantaloube J, Offner N, Csibi A, Leibovitch MP, Batonnet-Pichon S, Tintignac LA, Segura CT, Leibovitch SA (2008) The initiation factor eIF3-f is a major target for atrogin1/MAFbx function in skeletal muscle atrophy. EMBO J 27(8):1266-1276. doi: 10.1038/emboj.2008.52
    • (2008) EMBO J , vol.27 , Issue.8 , pp. 1266-1276
    • Lagirand-Cantaloube, J.1    Offner, N.2    Csibi, A.3    Leibovitch, M.P.4    Batonnet-Pichon, S.5    Tintignac, L.A.6    Segura, C.T.7    Leibovitch, S.A.8
  • 92
    • 78649917229 scopus 로고    scopus 로고
    • The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation
    • 10.1371/journal.pbio.1000545 21124883 10.1371/journal.pbio.1000545
    • Moretti J, Chastagner P, Gastaldello S, Heuss SF, Dirac AM, Bernards R, Masucci MG, Israel A, Brou C (2010) The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation. PLoS Biol 8(11):e1000545. doi: 10.1371/journal.pbio.1000545
    • (2010) PLoS Biol , vol.8 , Issue.11 , pp. 1000545
    • Moretti, J.1    Chastagner, P.2    Gastaldello, S.3    Heuss, S.F.4    Dirac, A.M.5    Bernards, R.6    Masucci, M.G.7    Israel, A.8    Brou, C.9
  • 93
    • 0030626959 scopus 로고    scopus 로고
    • The regulation of gene expression in hypertrophying skeletal muscle
    • 9213096 10.1249/00003677-199700250-00013 1:STN:280:DyaK2szls1Klsg%3D%3D
    • Carson JA (1997) The regulation of gene expression in hypertrophying skeletal muscle. Exerc Sport Sci Rev 25:301-320
    • (1997) Exerc Sport Sci Rev , vol.25 , pp. 301-320
    • Carson, J.A.1
  • 94
    • 0032948278 scopus 로고    scopus 로고
    • Phosphorylation of p70(S6 k) correlates with increased skeletal muscle mass following resistance exercise
    • 9886927 1:CAS:528:DyaK1MXnt12qtw%3D%3D
    • Baar K, Esser K (1999) Phosphorylation of p70(S6 k) correlates with increased skeletal muscle mass following resistance exercise. Am J Physiol 276(1 Pt 1):C120-C127
    • (1999) Am J Physiol , vol.276 , Issue.1 PART 1
    • Baar, K.1    Esser, K.2


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