메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Investigating the Consequences of eIF4E2 (4EHP) Interaction with 4E-Transporter on Its Cellular Distribution in HeLa Cells

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC TRIOXIDE; BINDING PROTEIN; CAP BINDING PROTEIN; DACTINOMYCIN; EIF4E TRANSPORTER PROTEIN; EIF4E1 PROTEIN; EIF4E2 PROTEIN; EXPORTIN 1; UNCLASSIFIED DRUG;

EID: 84882645365     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072761     Document Type: Article
Times cited : (23)

References (63)
  • 1
    • 77956275419 scopus 로고    scopus 로고
    • eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression
    • doi: 10.1073/pnas.1005320107
    • Furic L, Rong L, Larsson O, Koumakpayi IH, Yoshida K, et al. (2010) eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression. Proc Natl Acad Sci USA 107: 14134-14139. doi:10.1073/pnas.1005320107. PubMed: 20679199.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14134-14139
    • Furic, L.1    Rong, L.2    Larsson, O.3    Koumakpayi, I.H.4    Yoshida, K.5
  • 2
    • 2442648845 scopus 로고    scopus 로고
    • The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
    • doi: 10.1038/nm1042
    • Ruggero D, Montanaro L, Ma L, Xu W, Londei P, et al. (2004) The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nat Med 10: 484-486. doi:10.1038/nm1042. PubMed: 15098029.
    • (2004) Nat Med , vol.10 , pp. 484-486
    • Ruggero, D.1    Montanaro, L.2    Ma, L.3    Xu, W.4    Londei, P.5
  • 3
    • 84872617263 scopus 로고    scopus 로고
    • Exaggerated translation causes synaptic and behavioural aberrations associated with autism
    • 23172145
    • Santini E, Huynh TN, MacAskill AF, Carter AG, Pierre P, et al. (2013) Exaggerated translation causes synaptic and behavioural aberrations associated with autism. Nature 493: 371-377. PubMed: 23172145.
    • (2013) Nature , vol.493 , pp. 371-377
    • Santini, E.1    Huynh, T.N.2    MacAskill, A.F.3    Carter, A.G.4    Pierre, P.5
  • 4
    • 84872610247 scopus 로고    scopus 로고
    • Autism-related deficits via dysregulated eIF4E-dependent translational control
    • 23172145 (. (2013))
    • Gkogkas CG, Khoutorsky A, Ran I, Rampakakis E, Nevarko T, et al. (2012) Autism-related deficits via dysregulated eIF4E-dependent translational control. Nature (. (2013)) PubMed: 23172145.
    • (2012) Nature
    • Gkogkas, C.G.1    Khoutorsky, A.2    Ran, I.3    Rampakakis, E.4    Nevarko, T.5
  • 5
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • doi: 10.1038/nrm2838
    • Jackson RJ, Hellen CU, Pestova TV, (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11: 113-127. doi:10.1038/nrm2838. PubMed: 20094052.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 6
    • 84861843696 scopus 로고    scopus 로고
    • A mechanistic overview of translation initiation in eukaryotes
    • doi: 10.1038/nsmb.2303
    • Aitken CE, Lorsch JR, (2012) A mechanistic overview of translation initiation in eukaryotes. Nat Struct Mol Biol 19: 568-576. doi:10.1038/nsmb.2303. PubMed: 22664984.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 568-576
    • Aitken, C.E.1    Lorsch, J.R.2
  • 7
    • 84861231813 scopus 로고    scopus 로고
    • Translational control in cellular and developmental processes
    • doi: 10.1038/nrg3184
    • Kong J, Lasko P, (2012) Translational control in cellular and developmental processes. Nat Rev Genet 13: 383-394. doi:10.1038/nrg3184. PubMed: 22568971.
    • (2012) Nat Rev Genet , vol.13 , pp. 383-394
    • Kong, J.1    Lasko, P.2
  • 8
    • 15944389880 scopus 로고    scopus 로고
    • Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila
    • doi: 10.1016/j.mod.2004.11.011
    • Hernández G, Altmann M, Sierra JM, Urlaub H, del Corral RD, et al. (2005) Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila. Mech Dev 122: 529-543. doi:10.1016/j.mod.2004.11.011. PubMed: 15804566.
    • (2005) Mech Dev , vol.122 , pp. 529-543
    • Hernández, G.1    Altmann, M.2    Sierra, J.M.3    Urlaub, H.4    del Corral, R.D.5
  • 10
    • 0034616135 scopus 로고    scopus 로고
    • Functional characterization of five eIF4E isoforms in Caenorhabditis elegans
    • doi: 10.1074/jbc.275.14.10590
    • Keiper BD, Lamphear BJ, Deshpande AM, ankowska-Anyszka M, Aamodt EJ, et al. (2000) Functional characterization of five eIF4E isoforms in Caenorhabditis elegans. J Biol Chem 275: 10590-10596. doi:10.1074/jbc.275.14.10590. PubMed: 10744754.
    • (2000) J Biol Chem , vol.275 , pp. 10590-10596
    • Keiper, B.D.1    Lamphear, B.J.2    Deshpande, A.M.3    Ankowska-Anyszka, M.4    Aamodt, E.J.5
  • 11
    • 67650543838 scopus 로고    scopus 로고
    • eIF4E: new family members, new binding partners, new roles
    • doi: 10.1074/jbc.R900002200
    • Rhoads RE, (2009) eIF4E: new family members, new binding partners, new roles. J Biol Chem 284: 16711-16715. doi:10.1074/jbc.R900002200. PubMed: 19237539.
    • (2009) J Biol Chem , vol.284 , pp. 16711-16715
    • Rhoads, R.E.1
  • 12
    • 2942522541 scopus 로고    scopus 로고
    • Characterization of mammalian eIF4E-family members
    • doi: 10.1111/j.1432-1033.2004.04149.x
    • Joshi B, Cameron A, Jagus R, (2004) Characterization of mammalian eIF4E-family members. Eur J Biochem 271: 2189-2203. doi:10.1111/j.1432-1033.2004.04149.x. PubMed: 15153109.
    • (2004) Eur J Biochem , vol.271 , pp. 2189-2203
    • Joshi, B.1    Cameron, A.2    Jagus, R.3
  • 13
    • 27244447418 scopus 로고    scopus 로고
    • Phylogenetic analysis of eIF4E-family members
    • doi: 10.1186/1471-2148-5-48
    • Joshi B, Lee K, Maeder DL, Jagus R, (2005) Phylogenetic analysis of eIF4E-family members. BMC Evol Biol 5: 48. doi:10.1186/1471-2148-5-48. PubMed: 16191198.
    • (2005) BMC Evol Biol , vol.5 , pp. 48
    • Joshi, B.1    Lee, K.2    Maeder, D.L.3    Jagus, R.4
  • 14
    • 14444274091 scopus 로고    scopus 로고
    • Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein
    • doi: 10.1074/jbc.273.21.13104
    • Rom E, Kim HC, Gingras AC, [!(surname)!], Favre D, et al. (1998) Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein. J Biol Chem 273: 13104-13109. doi:10.1074/jbc.273.21.13104. PubMed: 9582349.
    • (1998) J Biol Chem , vol.273 , pp. 13104-13109
    • Rom, E.1    Kim, H.C.2    Gingras, A.C.3    Favre, D.4
  • 15
    • 34047174539 scopus 로고    scopus 로고
    • Structures of the Human eIF4E Homologous Protein, h4EHP, in its m(7)GTP-bound and Unliganded Forms
    • doi: 10.1016/j.jmb.2007.02.019
    • Rosettani P, Knapp S, Vismara MG, Rusconi L, Cameron AD, (2007) Structures of the Human eIF4E Homologous Protein, h4EHP, in its m(7)GTP-bound and Unliganded Forms. J Mol Biol 368: 691-705. doi:10.1016/j.jmb.2007.02.019. PubMed: 17368478.
    • (2007) J Mol Biol , vol.368 , pp. 691-705
    • Rosettani, P.1    Knapp, S.2    Vismara, M.G.3    Rusconi, L.4    Cameron, A.D.5
  • 16
    • 34247393290 scopus 로고    scopus 로고
    • Weak binding affinity of human 4EHP for mRNA cap analogs
    • doi: 10.1261/rna.453107
    • Zuberek J, Kubacka D, Jablonowska A, Jemielity J, Stepinski J, et al. (2007) Weak binding affinity of human 4EHP for mRNA cap analogs. RNA 13: 691-697. doi:10.1261/rna.453107. PubMed: 17369309.
    • (2007) RNA , vol.13 , pp. 691-697
    • Zuberek, J.1    Kubacka, D.2    Jablonowska, A.3    Jemielity, J.4    Stepinski, J.5
  • 17
    • 18844397041 scopus 로고    scopus 로고
    • A New Paradigm for Translational Control: Inhibition via -3 mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • doi: 10.1016/j.cell.2005.02.024
    • Cho PF, Poulin F, Cho-Park YA, Cho-Park IB, Chicoine JD, et al. (2005) A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell 121: 411-423 doi:10.1016/j.cell.2005.02.024. PubMed: 15882623.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5
  • 18
    • 65249118749 scopus 로고    scopus 로고
    • Cytoplasmic Prep1 interacts with 4EHP inhibiting Hoxb4 translation
    • doi: 10.1371/journal.pone.0005213
    • Villaescusa JC, Buratti C, Penkov D, Mathiasen L, Planagumà J, et al. (2009) Cytoplasmic Prep1 interacts with 4EHP inhibiting Hoxb4 translation. PLOS ONE 4: e5213. doi:10.1371/journal.pone.0005213. PubMed: 19365557.
    • (2009) PLOS ONE , vol.4
    • Villaescusa, J.C.1    Buratti, C.2    Penkov, D.3    Mathiasen, L.4    Planagumà, J.5
  • 19
    • 84866274906 scopus 로고    scopus 로고
    • A Novel 4EHP-GIGYF2 Translational Repressor Complex Is Essential for Mammalian Development
    • Morita M, Ler LW, Fabian MR, Siddiqui N, Mullin M, et al. (2012) A Novel 4EHP-GIGYF2 Translational Repressor Complex Is Essential for Mammalian Development. Mol Cell Biol 32: 3585-3593.
    • (2012) Mol Cell Biol , vol.32 , pp. 3585-3593
    • Morita, M.1    Ler, L.W.2    Fabian, M.R.3    Siddiqui, N.4    Mullin, M.5
  • 20
    • 0034660062 scopus 로고    scopus 로고
    • A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E
    • doi: 10.1093/emboj/19.12.3142
    • Dostie J, Ferraiuolo M, Pause A, Adam SA, Sonenberg N, (2000) A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E. EMBO J 19: 3142-3156. doi:10.1093/emboj/19.12.3142. PubMed: 10856257.
    • (2000) EMBO J , vol.19 , pp. 3142-3156
    • Dostie, J.1    Ferraiuolo, M.2    Pause, A.3    Adam, S.A.4    Sonenberg, N.5
  • 21
    • 24944448262 scopus 로고    scopus 로고
    • A role for the eIF4E-binding protein in P-body formation and mRNA decay
    • doi: 10.1083/jcb.200504039
    • Ferraiuolo MA, Basak S, Dostie J, Murray EL, Schoenberg DR, et al. (2005) A role for the eIF4E-binding protein in P-body formation and mRNA decay. J Cell Biol 170: 913-924. doi:10.1083/jcb.200504039. PubMed: 16157702.
    • (2005) J Cell Biol , vol.170 , pp. 913-924
    • Ferraiuolo, M.A.1    Basak, S.2    Dostie, J.3    Murray, E.L.4    Schoenberg, D.R.5
  • 22
    • 17844371700 scopus 로고    scopus 로고
    • A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    • doi: 10.1261/rna.2340405
    • Andrei MA, Ingelfinger D, Heintzmann R, Achsel T, Rivera-Pomar R, et al. (2005) A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA 11: 717-727. doi:10.1261/rna.2340405. PubMed: 15840819.
    • (2005) RNA , vol.11 , pp. 717-727
    • Andrei, M.A.1    Ingelfinger, D.2    Heintzmann, R.3    Achsel, T.4    Rivera-Pomar, R.5
  • 23
    • 41149176379 scopus 로고    scopus 로고
    • Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation
    • doi: 10.1016/j.bbrc.2008.03.017
    • Lee HC, Cho H, Kim YK, (2008) Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation. Biochem Biophys Res Commun 369: 1160-1165. doi:10.1016/j.bbrc.2008.03.017. PubMed: 18343217.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 1160-1165
    • Lee, H.C.1    Cho, H.2    Kim, Y.K.3
  • 24
    • 33845809231 scopus 로고    scopus 로고
    • P bodies: at the crossroads of post-transcriptional pathways
    • doi: 10.1038/nrg1981
    • Eulalio A, Behm-Ansmant I, Izaurralde E, (2007) P bodies: at the crossroads of post-transcriptional pathways. Nat Rev Mol Cell Biol 8: 9-22. doi:10.1038/nrg1981. PubMed: 17183357.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 9-22
    • Eulalio, A.1    Behm-Ansmant, I.2    Izaurralde, E.3
  • 25
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • doi: 10.1016/j.molcel.2007.02.011
    • Parker R, Sheth U, (2007) P bodies and the control of mRNA translation and degradation. Mol Cell 25: 635-646. doi:10.1016/j.molcel.2007.02.011. PubMed: 17349952.
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 26
    • 76449099716 scopus 로고    scopus 로고
    • On track with P-bodies
    • doi: 10.1042/BST0380242
    • Kulkarni M, Ozgur S, Stoecklin G, (2010) On track with P-bodies. Biochem Soc Trans 38: 242-251. doi:10.1042/BST0380242. PubMed: 20074068.
    • (2010) Biochem Soc Trans , vol.38 , pp. 242-251
    • Kulkarni, M.1    Ozgur, S.2    Stoecklin, G.3
  • 27
    • 38049134877 scopus 로고    scopus 로고
    • CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes
    • doi: 10.1074/jbc.M704629200
    • Minshall N, Reiter M-H, Weil D, Standart N, (2007) CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes. J Biol Chem 282: 37389-37401. doi:10.1074/jbc.M704629200. PubMed: 17942399.
    • (2007) J Biol Chem , vol.282 , pp. 37389-37401
    • Minshall, N.1    Reiter, M.-H.2    Weil, D.3    Standart, N.4
  • 28
    • 65649125183 scopus 로고    scopus 로고
    • Role of p54 RNA helicase activity and its C-terminal domain in translational repression, P-body localization and assembly
    • doi: 10.1091/mbc.E09-01-0035
    • Minshall N, Kress M, Weil D, Standart N, (2009) Role of p54 RNA helicase activity and its C-terminal domain in translational repression, P-body localization and assembly. Mol Biol Cell 20: 2464-2472. doi:10.1091/mbc.E09-01-0035. PubMed: 19297524.
    • (2009) Mol Biol Cell , vol.20 , pp. 2464-2472
    • Minshall, N.1    Kress, M.2    Weil, D.3    Standart, N.4
  • 29
    • 84866520245 scopus 로고    scopus 로고
    • The CPEB-family of proteins, translational control in senescence and cancer
    • doi: 10.1016/j.arr.2012.03.004
    • Fernández-Miranda G, Méndez R, (2012) The CPEB-family of proteins, translational control in senescence and cancer. Ageing Res Rev 11: 460-472. doi:10.1016/j.arr.2012.03.004. PubMed: 22542725.
    • (2012) Ageing Res Rev , vol.11 , pp. 460-472
    • Fernández-Miranda, G.1    Méndez, R.2
  • 30
    • 84861911071 scopus 로고    scopus 로고
    • Translational control by changes in poly(A) tail length: recycling mRNAs
    • doi: 10.1038/nsmb.2311
    • Weill L, Belloc E, Bava FA, Méndez R, (2012) Translational control by changes in poly(A) tail length: recycling mRNAs. Nat Struct Mol Biol 19: 577-585. doi:10.1038/nsmb.2311. PubMed: 22664985.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 577-585
    • Weill, L.1    Belloc, E.2    Bava, F.A.3    Méndez, R.4
  • 31
    • 60349132210 scopus 로고    scopus 로고
    • Evolutionary origin and phylogenetic analysis of the novel oocyte-specific eukaryotic translation initiation factor 4E in Tetrapoda
    • doi: 10.1007/s00427-008-0268-2
    • Evsikov AV, Marín de Evsikova C, (2009) Evolutionary origin and phylogenetic analysis of the novel oocyte-specific eukaryotic translation initiation factor 4E in Tetrapoda. Dev Genes Evol 219: 111-118. doi:10.1007/s00427-008-0268-2. PubMed: 19089447.
    • (2009) Dev Genes Evol , vol.219 , pp. 111-118
    • Evsikov, A.V.1    de Marín, E.C.2
  • 32
    • 49349088194 scopus 로고    scopus 로고
    • Translational control in early development: CPEB, P-bodies and germinal granules
    • doi: 10.1042/BST0360671
    • Standart N, Minshall N, (2008) Translational control in early development: CPEB, P-bodies and germinal granules. Biochem Soc Trans 36: 671-676. doi:10.1042/BST0360671. PubMed: 18631138.
    • (2008) Biochem Soc Trans , vol.36 , pp. 671-676
    • Standart, N.1    Minshall, N.2
  • 33
    • 0346503888 scopus 로고    scopus 로고
    • Drosophila Cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis
    • doi: 10.1016/S1534-5807(03)00400-3
    • Nakamura A, Sato K, Hanyu-Nakamura K, (2004) Drosophila Cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis. Dev Cell 6: 69-78. doi:10.1016/S1534-5807(03)00400-3. PubMed: 14723848.
    • (2004) Dev Cell , vol.6 , pp. 69-78
    • Nakamura, A.1    Sato, K.2    Hanyu-Nakamura, K.3
  • 34
    • 0842328579 scopus 로고    scopus 로고
    • Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression
    • doi: 10.1038/sj.emboj.7600026
    • Nelson MR, Leidal AM, Smibert CA, (2004) Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression. EMBO J 23: 150-159. doi:10.1038/sj.emboj.7600026. PubMed: 14685270.
    • (2004) EMBO J , vol.23 , pp. 150-159
    • Nelson, M.R.1    Leidal, A.M.2    Smibert, C.A.3
  • 35
    • 78149338276 scopus 로고    scopus 로고
    • Distinct functions of maternal and somatic Pat1 protein paralogs
    • doi: 10.1261/rna.2295410
    • Marnef A, Maldonado M, Bugaut A, Balasubramanian S, Kress M, et al. (2010) Distinct functions of maternal and somatic Pat1 protein paralogs. RNA 16: 2094-2107. doi:10.1261/rna.2295410. PubMed: 20826699.
    • (2010) RNA , vol.16 , pp. 2094-2107
    • Marnef, A.1    Maldonado, M.2    Bugaut, A.3    Balasubramanian, S.4    Kress, M.5
  • 36
    • 16844365216 scopus 로고    scopus 로고
    • The translational regulator CPEB1 provides a link between Dcp1 bodies and stress granules
    • doi: 10.1242/jcs.01692
    • Wilczynska A, Aigueperse C, Kress M, Dautry F, Weil D, (2005) The translational regulator CPEB1 provides a link between Dcp1 bodies and stress granules. J Cell Sci 118: 981-992. doi:10.1242/jcs.01692. PubMed: 15731006.
    • (2005) J Cell Sci , vol.118 , pp. 981-992
    • Wilczynska, A.1    Aigueperse, C.2    Kress, M.3    Dautry, F.4    Weil, D.5
  • 39
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • doi: 10.1038/nature10098
    • Schwanhäusser B, Busse D, Li N, Dittmar G, Schuchhardt J, et al. (2011) Global quantification of mammalian gene expression control. Nature 473: 337-342. doi:10.1038/nature10098. PubMed: 21593866.
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhäusser, B.1    Busse, D.2    Li, N.3    Dittmar, G.4    Schuchhardt, J.5
  • 40
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • doi: 10.1038/nature04209
    • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, et al. (2005) Towards a proteome-scale map of the human protein-protein interaction network. Nature 437: 1173-1178. doi:10.1038/nature04209. PubMed: 16189514.
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1    Venkatesan, K.2    Hao, T.3    Hirozane-Kishikawa, T.4    Dricot, A.5
  • 41
    • 84868676397 scopus 로고    scopus 로고
    • 4E-T Phosphorylation by JNK Promotes Stress-dependent P-body Assembly
    • doi: 10.1128/MCB.00544-12
    • Cargnello M, Tcherkezian J, Dorn JF, Huttlin EL, Maddox PS, et al. (2012) 4E-T Phosphorylation by JNK Promotes Stress-dependent P-body Assembly. Mol Cell Biol 32: 4572-4584. doi:10.1128/MCB.00544-12. PubMed: 22966201.
    • (2012) Mol Cell Biol , vol.32 , pp. 4572-4584
    • Cargnello, M.1    Tcherkezian, J.2    Dorn, J.F.3    Huttlin, E.L.4    Maddox, P.S.5
  • 42
    • 80054911203 scopus 로고    scopus 로고
    • Identification and function of the second eIF4E-binding region in N-terminal domain of eIF4G: comparison with eIF4E-binding protein
    • doi: 10.1016/j.bbrc.2011.09.084
    • Umenaga Y, Paku KS, In Y, Ishida T, Tomoo K, (2011) Identification and function of the second eIF4E-binding region in N-terminal domain of eIF4G: comparison with eIF4E-binding protein. Biochem Biophys Res Commun 414: 462-467. doi:10.1016/j.bbrc.2011.09.084. PubMed: 21964297.
    • (2011) Biochem Biophys Res Commun , vol.414 , pp. 462-467
    • Umenaga, Y.1    Paku, K.S.2    In, Y.3    Ishida, T.4    Tomoo, K.5
  • 43
    • 84055178150 scopus 로고    scopus 로고
    • A conserved motif within the flexible C-terminus of the translational regulator 4E-BP is required for tight binding to the mRNA cap-binding protein eIF4E
    • doi: 10.1042/BJ20101481
    • Paku KS, Umenaga Y, Usui T, Fukuyo A, Mizuno A, et al. (2012) A conserved motif within the flexible C-terminus of the translational regulator 4E-BP is required for tight binding to the mRNA cap-binding protein eIF4E. Biochem J 441: 237-245. doi:10.1042/BJ20101481. PubMed: 21913890.
    • (2012) Biochem J , vol.441 , pp. 237-245
    • Paku, K.S.1    Umenaga, Y.2    Usui, T.3    Fukuyo, A.4    Mizuno, A.5
  • 44
    • 55949116385 scopus 로고    scopus 로고
    • Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes
    • Trinkle-Mulcahy L, Boulon S, Lam YW, Urcia R, F-M. B, et al. (2008) Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes. J Cell Biol 183: 223-239.
    • (2008) J Cell Biol , vol.183 , pp. 223-239
    • Trinkle-Mulcahy, L.1    Boulon, S.2    Lam, Y.W.3    Urcia, R.4
  • 45
    • 78650916742 scopus 로고    scopus 로고
    • Stabilizing the eIF4G1 α-helix increases its binding affinity with eIF4E: implications for peptidomimetic design strategies
    • doi: 10.1016/j.jmb.2010.10.045
    • Brown CJ, Lim JJ, Leonard T, Lim HC, Chia CS, et al. (2011) Stabilizing the eIF4G1 α-helix increases its binding affinity with eIF4E: implications for peptidomimetic design strategies. J Mol Biol 405: 736-753. doi:10.1016/j.jmb.2010.10.045. PubMed: 21094167.
    • (2011) J Mol Biol , vol.405 , pp. 736-753
    • Brown, C.J.1    Lim, J.J.2    Leonard, T.3    Lim, H.C.4    Chia, C.S.5
  • 46
    • 84865118901 scopus 로고    scopus 로고
    • Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression
    • doi: 10.1261/rna.033639.112
    • Kinkelin K, Veith K, Grünwald M, Bono F, (2012) Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression. RNA 18: 1624-1634. doi:10.1261/rna.033639.112. PubMed: 22832024.
    • (2012) RNA , vol.18 , pp. 1624-1634
    • Kinkelin, K.1    Veith, K.2    Grünwald, M.3    Bono, F.4
  • 47
    • 80052972576 scopus 로고    scopus 로고
    • CUP promotes deadenylation and inhibits decapping of mRNA targets
    • doi: 10.1101/gad.17136311
    • Igreja C, Izaurralde E, (2011) CUP promotes deadenylation and inhibits decapping of mRNA targets. Genes Dev 25: 1955-1967. doi:10.1101/gad.17136311. PubMed: 21937713.
    • (2011) Genes Dev , vol.25 , pp. 1955-1967
    • Igreja, C.1    Izaurralde, E.2
  • 48
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • doi: 10.1016/S0076-6879(07)31005-7
    • Kedersha N, Anderson P, (2007) Mammalian stress granules and processing bodies. Methods Enzymol 431: 61-81. doi:10.1016/S0076-6879(07)31005-7. PubMed: 17923231.
    • (2007) Methods Enzymol , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 49
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: possible roles in the control of translation and mRNA degradation
    • doi: 10.1101/cshperspect.a012286
    • Decker CJ, Parker R, (2012) P-bodies and stress granules: possible roles in the control of translation and mRNA degradation. Cold Spring Harb Perspect Biol 4: a012286. doi:10.1101/cshperspect.a012286. PubMed: 22763747.
    • (2012) Cold Spring Harb Perspect Biol , vol.4
    • Decker, C.J.1    Parker, R.2
  • 50
    • 57349158716 scopus 로고    scopus 로고
    • Translationally repressed mRNA transiently cycles through stress granules during stress
    • doi: 10.1091/mbc.E08-05-0499
    • Mollet S, Cougot N, Wilczynska A, Dautry F, Kress M, et al. (2008) Translationally repressed mRNA transiently cycles through stress granules during stress. Mol Biol Cell 19: 4469-4479. doi:10.1091/mbc.E08-05-0499. PubMed: 18632980.
    • (2008) Mol Biol Cell , vol.19 , pp. 4469-4479
    • Mollet, S.1    Cougot, N.2    Wilczynska, A.3    Dautry, F.4    Kress, M.5
  • 51
    • 84855394456 scopus 로고    scopus 로고
    • RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor
    • Marnef A, Weil D, Standart N, (2012) RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor. Mol Biol Cell 23: 213-224.
    • (2012) Mol Biol Cell , vol.23 , pp. 213-224
    • Marnef, A.1    Weil, D.2    Standart, N.3
  • 52
    • 84865441580 scopus 로고    scopus 로고
    • Inhibition of mRNA maturation in trypanosomes causes the formation of novel foci at the nuclear periphery containing cytoplasmic regulators of mRNA fate
    • doi: 10.1242/jcs.099275
    • Kramer S, Marnef A, Standart N, Carrington M, (2012) Inhibition of mRNA maturation in trypanosomes causes the formation of novel foci at the nuclear periphery containing cytoplasmic regulators of mRNA fate. J Cell Sci 125: 2896-2909. doi:10.1242/jcs.099275. PubMed: 22366449.
    • (2012) J Cell Sci , vol.125 , pp. 2896-2909
    • Kramer, S.1    Marnef, A.2    Standart, N.3    Carrington, M.4
  • 53
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • doi: 10.1016/S0092-8674(00)80370-0
    • Stade K, Ford CS, Guthrie C, Weis K, (1997) Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90: 1041-1050. doi:10.1016/S0092-8674(00)80370-0. PubMed: 9323132.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 54
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: born to be weak
    • doi: 10.1016/j.tcb.2005.01.005
    • Kutay U, Güttinger S, (2005) Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol 15: 121-124. doi:10.1016/j.tcb.2005.01.005. PubMed: 15752974.
    • (2005) Trends Cell Biol , vol.15 , pp. 121-124
    • Kutay, U.1    Güttinger, S.2
  • 55
    • 45749141224 scopus 로고    scopus 로고
    • Control of eIF4E cellular localization by eIF4E-binding proteins, 4E-BPs
    • doi: 10.1261/rna.950608
    • Rong L, Livingstone M, Sukarieh R, Petroulakis E, Gingras AC, et al. (2008) Control of eIF4E cellular localization by eIF4E-binding proteins, 4E-BPs. RNA 14: 1318-1327. doi:10.1261/rna.950608. PubMed: 18515545.
    • (2008) RNA , vol.14 , pp. 1318-1327
    • Rong, L.1    Livingstone, M.2    Sukarieh, R.3    Petroulakis, E.4    Gingras, A.C.5
  • 56
    • 84865803029 scopus 로고    scopus 로고
    • The Oncogene eIF4E Reprograms the Nuclear Pore Complex to Promote mRNA Export and Oncogenic Transformation
    • doi: 10.1016/j.celrep.2012.07.007
    • Culjkovic-Kraljacic B, Baguet A, Volpon L, Amri A, Borden KL, (2012) The Oncogene eIF4E Reprograms the Nuclear Pore Complex to Promote mRNA Export and Oncogenic Transformation. Cell Rep 2: 207-215. doi:10.1016/j.celrep.2012.07.007. PubMed: 22902403.
    • (2012) Cell Rep , vol.2 , pp. 207-215
    • Culjkovic-Kraljacic, B.1    Baguet, A.2    Volpon, L.3    Amri, A.4    Borden, K.L.5
  • 57
    • 84861944874 scopus 로고    scopus 로고
    • An oxygen-regulated switch in the protein synthesis machinery
    • 22678294
    • Uniacke J, Holterman CE, Lachance G, Franovic A, Jacob MD, et al. (2012) An oxygen-regulated switch in the protein synthesis machinery. Nature 486: 126-129. PubMed: 22678294.
    • (2012) Nature , vol.486 , pp. 126-129
    • Uniacke, J.1    Holterman, C.E.2    Lachance, G.3    Franovic, A.4    Jacob, M.D.5
  • 58
    • 84862979524 scopus 로고    scopus 로고
    • Translational homeostasis via the mRNA cap-binding protein, eIF4E
    • doi: 10.1016/j.molcel.2012.04.004
    • Yanagiya A, Suyama E, Adachi H, Svitkin YV, Aza-Blanc P, et al. (2012) Translational homeostasis via the mRNA cap-binding protein, eIF4E. Mol Cell 46: 847-858. doi:10.1016/j.molcel.2012.04.004. PubMed: 22578813.
    • (2012) Mol Cell , vol.46 , pp. 847-858
    • Yanagiya, A.1    Suyama, E.2    Adachi, H.3    Svitkin, Y.V.4    Aza-Blanc, P.5
  • 59
    • 84861997955 scopus 로고    scopus 로고
    • The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts
    • doi: 10.1016/j.molcel.2012.05.021
    • Baltz AG, Munschauer M, Schwanhäusser B, Vasile A, Murakawa Y, et al. (2012) The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts. Mol Cell 46: 674-690. doi:10.1016/j.molcel.2012.05.021. PubMed: 22681889.
    • (2012) Mol Cell , vol.46 , pp. 674-690
    • Baltz, A.G.1    Munschauer, M.2    Schwanhäusser, B.3    Vasile, A.4    Murakawa, Y.5
  • 60
    • 84861969926 scopus 로고    scopus 로고
    • Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
    • doi: 10.1016/j.cell.2012.04.031
    • Castello A, Fischer B, Eichelbaum K, Horos R, Beckmann BM, et al. (2012) Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins. Cell 149: 1393-1406. doi:10.1016/j.cell.2012.04.031. PubMed: 22658674.
    • (2012) Cell , vol.149 , pp. 1393-1406
    • Castello, A.1    Fischer, B.2    Eichelbaum, K.3    Horos, R.4    Beckmann, B.M.5
  • 61
    • 0242541653 scopus 로고    scopus 로고
    • Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP
    • doi: 10.1016/S0014-5793(03)01235-3
    • Tan NG, Ardley HC, Scott GB, Rose SA, Markham AF, et al. (2003) Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP. FEBS Lett 554: 501-504. doi:10.1016/S0014-5793(03)01235-3. PubMed: 14623119.
    • (2003) FEBS Lett , vol.554 , pp. 501-504
    • Tan, N.G.1    Ardley, H.C.2    Scott, G.B.3    Rose, S.A.4    Markham, A.F.5
  • 62
    • 33847001685 scopus 로고    scopus 로고
    • ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP
    • doi: 10.1101/gad.1521607
    • Okumura F, Zou W, Zhang DE, (2007) ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP. Genes Dev 21: 255-260. doi:10.1101/gad.1521607. PubMed: 17289916.
    • (2007) Genes Dev , vol.21 , pp. 255-260
    • Okumura, F.1    Zou, W.2    Zhang, D.E.3
  • 63
    • 0030832026 scopus 로고    scopus 로고
    • eIF4G dramatically enhances the binding of eIF4E to the mRNA 5'-cap structure
    • doi: 10.1074/jbc.272.35.21677
    • Haghighat A, Sonenberg N, (1997) eIF4G dramatically enhances the binding of eIF4E to the mRNA 5'-cap structure. J Biol Chem 272: 21677-21680. doi:10.1074/jbc.272.35.21677. PubMed: 9268293.
    • (1997) J Biol Chem , vol.272 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.