메뉴 건너뛰기




Volumn 31, Issue 10, 2006, Pages 553-562

eIF3: a versatile scaffold for translation initiation complexes

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 3; MESSENGER RNA; METHIONINE; PROTEIN TYROSINE KINASE; RIBOSOME RNA; RNA 40S; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 33748924333     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2006.08.005     Document Type: Review
Times cited : (318)

References (83)
  • 1
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • Sonenberg N., et al. (Ed), Cold Spring Harbor Laboratory Press
    • Hershey J.W.B., and Merrick W.C. Pathway and mechanism of initiation of protein synthesis. In: Sonenberg N., et al. (Ed). Translational Control of Gene Expression (2000), Cold Spring Harbor Laboratory Press 33-88
    • (2000) Translational Control of Gene Expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 2
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova T.V., and Kolupaeva V.G. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev. 16 (2002) 2906-2922
    • (2002) Genes Dev. , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 3
    • 26944435515 scopus 로고    scopus 로고
    • Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • Algire M.A., et al. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 20 (2005) 251-262
    • (2005) Mol. Cell , vol.20 , pp. 251-262
    • Algire, M.A.1
  • 4
    • 0037168583 scopus 로고    scopus 로고
    • Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation
    • Lee J.H., et al. Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16689-16694
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16689-16694
    • Lee, J.H.1
  • 5
    • 0002470681 scopus 로고    scopus 로고
    • Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes
    • Sonenberg N., et al. (Ed), Cold Spring Harbor Laboratory Press
    • Hinnebusch A.G. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. In: Sonenberg N., et al. (Ed). Translational Control of Gene Expression (2000), Cold Spring Harbor Laboratory Press 185-243
    • (2000) Translational Control of Gene Expression , pp. 185-243
    • Hinnebusch, A.G.1
  • 6
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H.P., et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6 (2000) 1099-1108
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1
  • 7
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras A.C., et al. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15 (2001) 807-826
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1
  • 8
    • 0030827905 scopus 로고    scopus 로고
    • Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits: possible roles in RNA binding and macromolecular assembly
    • Asano K., et al. Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits: possible roles in RNA binding and macromolecular assembly. J. Biol. Chem. 272 (1997) 27042-27052
    • (1997) J. Biol. Chem. , vol.272 , pp. 27042-27052
    • Asano, K.1
  • 9
    • 0030843398 scopus 로고    scopus 로고
    • The translation initiation factor eIF3-p48 subunit is encoded by int-6, a site of frequent integration by the mouse mammary tumor virus genome
    • Asano K., et al. The translation initiation factor eIF3-p48 subunit is encoded by int-6, a site of frequent integration by the mouse mammary tumor virus genome. J. Biol. Chem. 272 (1997) 23477-23480
    • (1997) J. Biol. Chem. , vol.272 , pp. 23477-23480
    • Asano, K.1
  • 10
    • 0035824649 scopus 로고    scopus 로고
    • The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3
    • Morris-Desbois C., et al. The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3. J. Biol. Chem. 276 (2001) 45988-45995
    • (2001) J. Biol. Chem. , vol.276 , pp. 45988-45995
    • Morris-Desbois, C.1
  • 11
    • 0035337708 scopus 로고    scopus 로고
    • Unified nomenclature for the subunits of eukaryotic initiation factor 3′
    • Browning K.S., et al. Unified nomenclature for the subunits of eukaryotic initiation factor 3′. Trends Biochem. Sci. 26 (2001) 284
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 284
    • Browning, K.S.1
  • 12
    • 0142057156 scopus 로고    scopus 로고
    • Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3
    • Mayeur G.L., et al. Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3. Eur. J. Biochem. 270 (2003) 4133-4139
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4133-4139
    • Mayeur, G.L.1
  • 13
    • 10644249220 scopus 로고    scopus 로고
    • Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP
    • Unbehaun A., et al. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev. 18 (2004) 3078-3093
    • (2004) Genes Dev. , vol.18 , pp. 3078-3093
    • Unbehaun, A.1
  • 14
    • 0031876171 scopus 로고    scopus 로고
    • Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
    • Phan L., et al. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol. 18 (1998) 4935-4946
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4935-4946
    • Phan, L.1
  • 15
    • 0032483390 scopus 로고    scopus 로고
    • Nip1p associates with 40S ribosomes and the Prt1p subunit of eIF3 and is required for efficient translation initiation
    • Greenberg J.R., et al. Nip1p associates with 40S ribosomes and the Prt1p subunit of eIF3 and is required for efficient translation initiation. J. Biol. Chem. 273 (1998) 23485-23494
    • (1998) J. Biol. Chem. , vol.273 , pp. 23485-23494
    • Greenberg, J.R.1
  • 16
    • 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
    • Valášek L., et al. Rpg1, the Saccharomyces cerevisiae homologue of the largest subunit of mammalian translation initiation factor 3, is required for translational activity. J. Biol. Chem. 273 (1998) 21253-21260
    • (1998) J. Biol. Chem. , vol.273 , pp. 21253-21260
    • Valášek, L.1
  • 17
    • 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
    • Naranda T., et al. 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 (1997) 145-153
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 145-153
    • Naranda, T.1
  • 18
    • 0033605753 scopus 로고    scopus 로고
    • Characterization of the p33 subunit of eukaryotic translation initiation factor-3 from Saccharomyces cerevisiae
    • Hanachi P., et al. Characterization of the p33 subunit of eukaryotic translation initiation factor-3 from Saccharomyces cerevisiae. J. Biol. Chem. 274 (1999) 8546-8553
    • (1999) J. Biol. Chem. , vol.274 , pp. 8546-8553
    • Hanachi, P.1
  • 19
    • 0030832613 scopus 로고    scopus 로고
    • Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation
    • Verlhac M.-H., et al. Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation. EMBO J. 16 (1997) 6812-6822
    • (1997) EMBO J. , vol.16 , pp. 6812-6822
    • Verlhac, M.-H.1
  • 20
    • 0032541138 scopus 로고    scopus 로고
    • Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae
    • Asano K., et al. Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 18573-18585
    • (1998) J. Biol. Chem. , vol.273 , pp. 18573-18585
    • Asano, K.1
  • 21
    • 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
    • Vornlocher H.P., et al. 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 (1999) 16802-16812
    • (1999) J. Biol. Chem. , vol.274 , pp. 16802-16812
    • Vornlocher, H.P.1
  • 22
    • 0039183713 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae HCRI gene encoding a homologue of the p35 subunit of human translation eukaryotic initiation factor 3 (eIF3) is a high copy suppressor of a temperature-sensitive mutation in the Rpg1p subunit of yeast eIF3
    • Valášek L., et al. The Saccharomyces cerevisiae HCRI gene encoding a homologue of the p35 subunit of human translation eukaryotic initiation factor 3 (eIF3) is a high copy suppressor of a temperature-sensitive mutation in the Rpg1p subunit of yeast eIF3. J. Biol. Chem. 274 (1999) 27567-27572
    • (1999) J. Biol. Chem. , vol.274 , pp. 27567-27572
    • Valášek, L.1
  • 23
    • 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
    • Valášek L., et al. Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding. EMBO J. 20 (2001) 891-904
    • (2001) EMBO J. , vol.20 , pp. 891-904
    • Valášek, L.1
  • 24
    • 0035900747 scopus 로고    scopus 로고
    • Dual function of eIF3j/Hcr1p in processing 20 S pre-rRNA and translation initiation
    • Valášek L., et al. Dual function of eIF3j/Hcr1p in processing 20 S pre-rRNA and translation initiation. J. Biol. Chem. 276 (2001) 43351-43360
    • (2001) J. Biol. Chem. , vol.276 , pp. 43351-43360
    • Valášek, L.1
  • 25
    • 33645841066 scopus 로고    scopus 로고
    • Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast
    • Nielsen K. Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast. Mol. Cell. Biol. 26 (2006) 2984-2998
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2984-2998
    • Nielsen, K.1
  • 26
    • 0035971249 scopus 로고    scopus 로고
    • Fission yeast homolog of murine Int-6 protein, encoded by mouse mammary tumor virus integration site, is associated with the conserved core subunits of eukaryotic translation initiation factor 3
    • Akiyoshi Y., et al. Fission yeast homolog of murine Int-6 protein, encoded by mouse mammary tumor virus integration site, is associated with the conserved core subunits of eukaryotic translation initiation factor 3. J. Biol. Chem. 276 (2000) 10056-10062
    • (2000) J. Biol. Chem. , vol.276 , pp. 10056-10062
    • Akiyoshi, Y.1
  • 27
    • 0033747046 scopus 로고    scopus 로고
    • + causes hypersensitivity to caffeine and affects spore formation
    • + causes hypersensitivity to caffeine and affects spore formation. Mol. Biol. Cell 11 (2000) 4005-4018
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4005-4018
    • Bandyopadhyay, A.1
  • 28
    • 0033582272 scopus 로고    scopus 로고
    • Moe1, a conserved protein in Schizosaccharomyces pombe, interacts with a Ras effector, Scd1, to affect proper spindle formation
    • Chen C.R., et al. Moe1, a conserved protein in Schizosaccharomyces pombe, interacts with a Ras effector, Scd1, to affect proper spindle formation. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 517-522
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 517-522
    • Chen, C.R.1
  • 29
    • 0033749641 scopus 로고    scopus 로고
    • A fission yeast homolog of int-6, the mammalian oncoprotein and eIF3 subunit, induces drug resistance when overexpressed
    • Crane R., et al. A fission yeast homolog of int-6, the mammalian oncoprotein and eIF3 subunit, induces drug resistance when overexpressed. Mol. Biol. Cell 11 (2000) 3993-4003
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3993-4003
    • Crane, R.1
  • 30
    • 27544510262 scopus 로고    scopus 로고
    • PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes
    • Zhou C., et al. PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes. BMC Biol. 3 (2005) 14
    • (2005) BMC Biol. , vol.3 , pp. 14
    • Zhou, C.1
  • 31
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valášek L., et al. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J. 21 (2002) 5886-5898
    • (2002) EMBO J. , vol.21 , pp. 5886-5898
    • Valášek, L.1
  • 32
    • 0031021584 scopus 로고    scopus 로고
    • The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170
    • Methot N., et al. The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170. J. Biol. Chem. 272 (1997) 1110-1116
    • (1997) J. Biol. Chem. , vol.272 , pp. 1110-1116
    • Methot, N.1
  • 33
    • 1542305510 scopus 로고    scopus 로고
    • The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40S ribosomal subunits in vitro
    • Fraser C.S., et al. The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40S ribosomal subunits in vitro. J. Biol. Chem. 279 (2004) 8946-8956
    • (2004) J. Biol. Chem. , vol.279 , pp. 8946-8956
    • Fraser, C.S.1
  • 34
    • 0242390528 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits
    • Shalev A., et al. Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits. J. Biol. Chem. 276 (2001) 34948-34957
    • (2001) J. Biol. Chem. , vol.276 , pp. 34948-34957
    • Shalev, A.1
  • 35
    • 0033580851 scopus 로고    scopus 로고
    • Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40S ribosomal preinitiation complex
    • Chaudhuri J., et al. Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40S ribosomal preinitiation complex. J. Biol. Chem. 274 (1999) 17975-17980
    • (1999) J. Biol. Chem. , vol.274 , pp. 17975-17980
    • Chaudhuri, J.1
  • 36
    • 10644277580 scopus 로고    scopus 로고
    • Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association
    • Kolupaeva V.G., et al. Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association. RNA 11 (2005) 470-486
    • (2005) RNA , vol.11 , pp. 470-486
    • Kolupaeva, V.G.1
  • 37
    • 0037458626 scopus 로고    scopus 로고
    • Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40S preinitiation complex
    • Majumdar R., et al. Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40S preinitiation complex. J. Biol. Chem. 278 (2003) 6580-6587
    • (2003) J. Biol. Chem. , vol.278 , pp. 6580-6587
    • Majumdar, R.1
  • 38
    • 0345305759 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing
    • Lomakin I.B., et al. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev. 17 (2003) 2786-2797
    • (2003) Genes Dev. , vol.17 , pp. 2786-2797
    • Lomakin, I.B.1
  • 39
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA ribosome and subunit-subunit interactions
    • Spahn C.M., et al. Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA ribosome and subunit-subunit interactions. Cell 107 (2001) 373-386
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1
  • 40
    • 0022704950 scopus 로고
    • Structure and location of initiation factor eIF-3 within native small ribosomal subunits from eukaryotes
    • Lutsch G., et al. Structure and location of initiation factor eIF-3 within native small ribosomal subunits from eukaryotes. Eur. J. Cell Biol. 40 (1986) 257-265
    • (1986) Eur. J. Cell Biol. , vol.40 , pp. 257-265
    • Lutsch, G.1
  • 41
    • 0026752980 scopus 로고
    • Eukaryotic initiation factor 3 does not prevent association through physical blockage of the ribosomal subunit-subunit interface
    • Srivastava S., et al. Eukaryotic initiation factor 3 does not prevent association through physical blockage of the ribosomal subunit-subunit interface. J. Mol. Biol. 220 (1992) 301-304
    • (1992) J. Mol. Biol. , vol.220 , pp. 301-304
    • Srivastava, S.1
  • 42
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a and NIP1/c and eIF5 make critical connections with the 40S ribosome in vivo
    • Valášek L., et al. The yeast eIF3 subunits TIF32/a and NIP1/c and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev. 17 (2003) 786-799
    • (2003) Genes Dev. , vol.17 , pp. 786-799
    • Valášek, L.1
  • 43
    • 28544439977 scopus 로고    scopus 로고
    • Structural roles for human translation factor eIF3 in initiation of protein synthesis
    • Siridechadilok B., et al. Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310 (2005) 1513-1515
    • (2005) Science , vol.310 , pp. 1513-1515
    • Siridechadilok, B.1
  • 44
    • 0032481304 scopus 로고    scopus 로고
    • Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis
    • Janosi L., et al. Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis. EMBO J. 17 (1998) 1141-1151
    • (1998) EMBO J. , vol.17 , pp. 1141-1151
    • Janosi, L.1
  • 45
    • 0020490386 scopus 로고
    • Specific interaction of one subunit of eukaryotic initiation factor eIF-3 with 18S rRNA within the binary complex, eIF-3-small ribosomal subunit, as shown by cross-linking experiments
    • Nygard O., and Westermann P. Specific interaction of one subunit of eukaryotic initiation factor eIF-3 with 18S rRNA within the binary complex, eIF-3-small ribosomal subunit, as shown by cross-linking experiments. Nucleic Acids Res. 10 (1982) 1327-1334
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1327-1334
    • Nygard, O.1    Westermann, P.2
  • 46
    • 23344438324 scopus 로고    scopus 로고
    • Changes in ribosomal binding activity of eIF3 correlate with increased translation rates during activation of T lymphocytes
    • Miyamoto S., et al. Changes in ribosomal binding activity of eIF3 correlate with increased translation rates during activation of T lymphocytes. J. Biol. Chem. 280 (2005) 28251-28264
    • (2005) J. Biol. Chem. , vol.280 , pp. 28251-28264
    • Miyamoto, S.1
  • 47
    • 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
    • Hui D.J., et al. 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 (2003) 39477-39482
    • (2003) J. Biol. Chem. , vol.278 , pp. 39477-39482
    • Hui, D.J.1
  • 48
    • 0036224032 scopus 로고    scopus 로고
    • Development and characterization of a reconstituted yeast translation initiation system
    • Algire M.A., et al. Development and characterization of a reconstituted yeast translation initiation system. RNA 8 (2002) 382-397
    • (2002) RNA , vol.8 , pp. 382-397
    • Algire, M.A.1
  • 49
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • Maag D., et al. A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon. Mol. Cell 17 (2005) 265-275
    • (2005) Mol. Cell , vol.17 , pp. 265-275
    • Maag, D.1
  • 50
    • 0028947302 scopus 로고
    • Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae
    • Danaie P., et al. Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae. J. Biol. Chem. 270 (1995) 4288-4292
    • (1995) J. Biol. Chem. , vol.270 , pp. 4288-4292
    • Danaie, P.1
  • 51
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano K., et al. Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J. 20 (2001) 2326-2337
    • (2001) EMBO J. , vol.20 , pp. 2326-2337
    • Asano, K.1
  • 52
    • 0035355352 scopus 로고    scopus 로고
    • Met
    • Met. EMBO J. 20 (2001) 2954-2965
    • (2001) EMBO J. , vol.20 , pp. 2954-2965
    • Phan, L.1
  • 53
    • 0034307347 scopus 로고    scopus 로고
    • Met is an important translation initiation intermediate in vivo
    • Met is an important translation initiation intermediate in vivo. Genes Dev. 14 (2000) 2534-2546
    • (2000) Genes Dev. , vol.14 , pp. 2534-2546
    • Asano, K.1
  • 54
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano K., et al. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18 (1999) 1673-1688
    • (1999) EMBO J. , vol.18 , pp. 1673-1688
    • Asano, K.1
  • 55
    • 3843096103 scopus 로고    scopus 로고
    • Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo
    • Singh C.R., et al. Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo. J. Biol. Chem. 279 (2004) 31910-31920
    • (2004) J. Biol. Chem. , vol.279 , pp. 31910-31920
    • Singh, C.R.1
  • 56
    • 1842576663 scopus 로고    scopus 로고
    • Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control
    • Nielsen K.H., et al. Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control. EMBO J. 23 (2004) 1166-1177
    • (2004) EMBO J. , vol.23 , pp. 1166-1177
    • Nielsen, K.H.1
  • 57
    • 6344291066 scopus 로고    scopus 로고
    • Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection
    • Valasek L., et al. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol. Cell. Biol. 24 (2004) 9437-9455
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9437-9455
    • Valasek, L.1
  • 58
    • 20744451862 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation
    • Singh C.R., et al. Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation. Mol. Cell. Biol. 25 (2005) 5480-5491
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5480-5491
    • Singh, C.R.1
  • 59
    • 28044445673 scopus 로고    scopus 로고
    • The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G
    • Yamamoto Y., et al. The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 16164-16169
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16164-16169
    • Yamamoto, Y.1
  • 60
    • 32044467711 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast
    • Jivotovskaya A.V., et al. Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast. Mol. Cell. Biol. 26 (2006) 1355-1372
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1355-1372
    • Jivotovskaya, A.V.1
  • 61
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases
    • Lamphear B.J., et al. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. J. Biol. Chem. 270 (1995) 21975-21983
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1
  • 62
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka H., and Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell. Biol. 17 (1997) 6940-6947
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 63
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region
    • Morino S., et al. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region. Mol. Cell. Biol. 20 (2000) 468-477
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 468-477
    • Morino, S.1
  • 64
    • 0034731347 scopus 로고    scopus 로고
    • Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1
    • Korneeva N.L., et al. Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1. J. Biol. Chem. 275 (2000) 41369-41376
    • (2000) J. Biol. Chem. , vol.275 , pp. 41369-41376
    • Korneeva, N.L.1
  • 65
    • 33646124490 scopus 로고    scopus 로고
    • mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin
    • Harris T.E., et al. mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin. EMBO J. 25 (2006) 1659-1668
    • (2006) EMBO J. , vol.25 , pp. 1659-1668
    • Harris, T.E.1
  • 66
    • 13544276792 scopus 로고    scopus 로고
    • Mouse p56 blocks a distinct function of eukaryotic initiation factor 3 in translation initiation
    • Hui D.J., et al. Mouse p56 blocks a distinct function of eukaryotic initiation factor 3 in translation initiation. J. Biol. Chem. 280 (2005) 3433-3440
    • (2005) J. Biol. Chem. , vol.280 , pp. 3433-3440
    • Hui, D.J.1
  • 67
    • 24944572189 scopus 로고    scopus 로고
    • eIF4G and CBP80 share a common origin and similar domain organization: implications for the structure and function of eIF4G
    • Marintchev A., and Wagner G. eIF4G and CBP80 share a common origin and similar domain organization: implications for the structure and function of eIF4G. Biochemistry 44 (2005) 12265-12272
    • (2005) Biochemistry , vol.44 , pp. 12265-12272
    • Marintchev, A.1    Wagner, G.2
  • 68
    • 27744569843 scopus 로고    scopus 로고
    • mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz M.K., et al. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123 (2005) 569-580
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1
  • 69
    • 0033610845 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3
    • Block K.L., et al. Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3. J. Biol. Chem. 273 (1998) 31901-31908
    • (1998) J. Biol. Chem. , vol.273 , pp. 31901-31908
    • Block, K.L.1
  • 70
    • 0031033314 scopus 로고    scopus 로고
    • Conservation and diversity of eukaryotic translation initiation factor eIF3
    • Asano K., et al. Conservation and diversity of eukaryotic translation initiation factor eIF3. J. Biol. Chem. 272 (1997) 1101-1109
    • (1997) J. Biol. Chem. , vol.272 , pp. 1101-1109
    • Asano, K.1
  • 71
    • 2342656309 scopus 로고    scopus 로고
    • Role of eIF3 p170 in controlling synthesis of ribonucleotide reductase M2 and cell growth
    • Dong Z., et al. Role of eIF3 p170 in controlling synthesis of ribonucleotide reductase M2 and cell growth. Oncogene 23 (2004) 3790-3801
    • (2004) Oncogene , vol.23 , pp. 3790-3801
    • Dong, Z.1
  • 72
    • 8844285955 scopus 로고    scopus 로고
    • 20S proteasome differentially alters translation of different mRNAs via the cleavage of eIF4F and eIF3
    • Baugh J.M., and Pilipenko E.V. 20S proteasome differentially alters translation of different mRNAs via the cleavage of eIF4F and eIF3. Mol. Cell 16 (2004) 575-586
    • (2004) Mol. Cell , vol.16 , pp. 575-586
    • Baugh, J.M.1    Pilipenko, E.V.2
  • 73
    • 21644490138 scopus 로고    scopus 로고
    • Translational regulation via 5′ mRNA leader sequences revealed by mutational analysis of the Arabidopsis translation initiation factor subunit eIF3h
    • Kim T.H., et al. Translational regulation via 5′ mRNA leader sequences revealed by mutational analysis of the Arabidopsis translation initiation factor subunit eIF3h. Plant Cell 16 (2004) 3341-3356
    • (2004) Plant Cell , vol.16 , pp. 3341-3356
    • Kim, T.H.1
  • 74
    • 0029805730 scopus 로고    scopus 로고
    • In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: the role of the RNA remotif
    • Methot N., et al. In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: the role of the RNA remotif. RNA 2 (1996) 38-50
    • (1996) RNA , vol.2 , pp. 38-50
    • Methot, N.1
  • 75
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYFG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3
    • Methot N., et al. A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYFG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol. Cell. Biol. 16 (1996) 5328-5334
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5328-5334
    • Methot, N.1
  • 76
    • 0033522507 scopus 로고    scopus 로고
    • Structure and interactions of the translation initiation factor eIF1
    • Fletcher C.M., et al. Structure and interactions of the translation initiation factor eIF1. EMBO J. 18 (1999) 2631-2639
    • (1999) EMBO J. , vol.18 , pp. 2631-2639
    • Fletcher, C.M.1
  • 77
    • 27744467413 scopus 로고    scopus 로고
    • Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation
    • Majumdar R., and Maitra U. Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation. EMBO J. 24 (2005) 3737-3746
    • (2005) EMBO J. , vol.24 , pp. 3737-3746
    • Majumdar, R.1    Maitra, U.2
  • 78
    • 0035929148 scopus 로고    scopus 로고
    • A plant viral 'reinitiation' factor interacts with the host translational machinery
    • Park H.S., et al. A plant viral 'reinitiation' factor interacts with the host translational machinery. Cell 106 (2001) 723-733
    • (2001) Cell , vol.106 , pp. 723-733
    • Park, H.S.1
  • 79
    • 1942439145 scopus 로고    scopus 로고
    • Eucaryotic initiation factor 4B controls eIF3-mediated ribosomal entry of viral reinitiation factor
    • Park H.S., et al. Eucaryotic initiation factor 4B controls eIF3-mediated ribosomal entry of viral reinitiation factor. EMBO J. 23 (2004) 1381-1391
    • (2004) EMBO J. , vol.23 , pp. 1381-1391
    • Park, H.S.1
  • 80
    • 0346497769 scopus 로고    scopus 로고
    • What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?
    • Poyry T.A., et al. What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?. Genes Dev. 18 (2004) 62-75
    • (2004) Genes Dev. , vol.18 , pp. 62-75
    • Poyry, T.A.1
  • 81
    • 0037675905 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit
    • Maag D., and Lorsch J.R. Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit. J. Mol. Biol. 330 (2003) 917-924
    • (2003) J. Mol. Biol. , vol.330 , pp. 917-924
    • Maag, D.1    Lorsch, J.R.2
  • 82
    • 0034801441 scopus 로고    scopus 로고
    • Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p
    • Palecek J., et al. Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p. Biochem. Biophys. Res. Commun. 282 (2001) 1244-1250
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 1244-1250
    • Palecek, J.1
  • 83
    • 0034955565 scopus 로고    scopus 로고
    • Two subcellular localizations of eIF3 p170 and its interaction with membrane-bound microfilaments: implications for alternative functions of p170
    • Pincheira R., et al. Two subcellular localizations of eIF3 p170 and its interaction with membrane-bound microfilaments: implications for alternative functions of p170. Eur. J. Cell Biol. 80 (2001) 410-418
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 410-418
    • Pincheira, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.