메뉴 건너뛰기




Volumn 32, Issue 17, 2012, Pages 3585-3593

A novel 4EHP-GIGYF2 translational repressor complex is essential for mammalian development

Author keywords

[No Author keywords available]

Indexed keywords

DROSOPHILA PROTEIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 10; GROWTH FACTOR RECEPTOR BOUND PROTEIN 10 INTERACTING GYF PROTEIN 2; INITIATION FACTOR 4E; INITIATION FACTOR 4E HOMOLOGOUS PROTEIN; MESSENGER RNA; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; ZINC FINGER PROTEIN 598;

EID: 84866274906     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00455-12     Document Type: Article
Times cited : (145)

References (47)
  • 1
    • 77955482621 scopus 로고    scopus 로고
    • Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes
    • Ash MR, et al. 2010. Conserved beta-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes. Structure 18:944-954.
    • (2010) Structure , vol.18 , pp. 944-954
    • Ash, M.R.1
  • 2
    • 32044471522 scopus 로고    scopus 로고
    • Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles
    • Chekulaeva M, Hentze MW, Ephrussi A. 2006. Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles. Cell 124:521-533.
    • (2006) Cell , vol.124 , pp. 521-533
    • Chekulaeva, M.1    Hentze, M.W.2    Ephrussi, A.3
  • 3
    • 57649174475 scopus 로고    scopus 로고
    • PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4
    • Chen GI, et al. 2008. PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4. J. Biol. Chem. 283:29273-29284.
    • (2008) J. Biol. Chem , vol.283 , pp. 29273-29284
    • Chen, G.I.1
  • 4
    • 33749989519 scopus 로고    scopus 로고
    • Cap- dependent translational inhibition establishes two opposing morphogen gradients in Drosophila embryos
    • Cho PF, et al. 2006. Cap-dependent translational inhibition establishes two opposing morphogen gradients in Drosophila embryos. Curr. Biol. 16:2035-2041.
    • (2006) Curr. Biol , vol.16 , pp. 2035-2041
    • Cho, P.F.1
  • 5
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho PF, 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.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1
  • 6
    • 11144323221 scopus 로고    scopus 로고
    • Translation of a small subset of Caenorhabditis elegans mRNAs is dependent on a specific eukaryotic translation initiation factor 4E isoform
    • Dinkova TD, Keiper BD, Korneeva NL, Aamodt EJ, Rhoads RE. 2005. Translation of a small subset of Caenorhabditis elegans mRNAs is dependent on a specific eukaryotic translation initiation factor 4E isoform. Mol. Cell. Biol. 25:100-113.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 100-113
    • Dinkova, T.D.1    Keiper, B.D.2    Korneeva, N.L.3    Aamodt, E.J.4    Rhoads, R.E.5
  • 7
    • 0034660062 scopus 로고    scopus 로고
    • A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E
    • 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.
    • (2000) EMBO J , vol.19 , pp. 3142-3156
    • Dostie, J.1    Ferraiuolo, M.2    Pause, A.3    Adam, S.A.4    Sonenberg, N.5
  • 8
    • 77952967459 scopus 로고    scopus 로고
    • mTORC1-mediated cell proliferation, but not cell growth, controlled by the 4E-BPs
    • Dowling RJ, et al. 2010. mTORC1-mediated cell proliferation, but not cell growth, controlled by the 4E-BPs. Science 328:1172-1176.
    • (2010) Science , vol.328 , pp. 1172-1176
    • Dowling, R.J.1
  • 9
    • 0024238770 scopus 로고
    • High-level synthesis in Escherichia coli of functional cap-binding eukaryotic initiation factor eIF-4E and affinity purification using a simplified cap-analog resin
    • Edery I, Altmann M, Sonenberg N. 1988. High-level synthesis in Escherichia coli of functional cap-binding eukaryotic initiation factor eIF-4E and affinity purification using a simplified cap-analog resin. Gene 74:517-525.
    • (1988) Gene , vol.74 , pp. 517-525
    • Edery, I.1    Altmann, M.2    Sonenberg, N.3
  • 10
    • 24944448262 scopus 로고    scopus 로고
    • A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay
    • Ferraiuolo MA, et al. 2005. A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay. J. Cell Biol. 170:913-924.
    • (2005) J. Cell Biol , vol.170 , pp. 913-924
    • Ferraiuolo, M.A.1
  • 11
    • 28644433887 scopus 로고    scopus 로고
    • A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity
    • Gingras AC, et al. 2005. A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity. Mol. Cell. Proteomics 4:1725-1740.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1725-1740
    • Gingras, A.C.1
  • 12
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism
    • Gingras AC, et al. 1999. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism. Genes Dev. 13:1422-1437.
    • (1999) Genes Dev , vol.13 , pp. 1422-1437
    • Gingras, A.C.1
  • 13
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N. 1999. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68:913-963.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 14
    • 0041355365 scopus 로고    scopus 로고
    • Two novel proteins that are linked to insulinlike growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling
    • Giovannone B, et al. 2003. Two novel proteins that are linked to insulinlike growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling. J. Biol. Chem. 278:31564-31573.
    • (2003) J. Biol. Chem , vol.278 , pp. 31564-31573
    • Giovannone, B.1
  • 15
    • 70449356621 scopus 로고    scopus 로고
    • GIGYF2 gene disruption in mice results in neurodegeneration and altered insulin-like growth factor signaling
    • Giovannone B, et al. 2009. GIGYF2 gene disruption in mice results in neurodegeneration and altered insulin-like growth factor signaling. Hum. Mol. Genet. 18:4629-4639.
    • (2009) Hum. Mol. Genet , vol.18 , pp. 4629-4639
    • Giovannone, B.1
  • 16
    • 59149096171 scopus 로고    scopus 로고
    • A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein
    • Goudreault M, et al. 2009. A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein. Mol. Cell. Proteomics 8:157-171.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 157-171
    • Goudreault, M.1
  • 17
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1 competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat A, Mader S, Pause A, Sonenberg N. 1995. Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J. 14:5701-5709.
    • (1995) EMBO J , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 18
    • 78651325259 scopus 로고    scopus 로고
    • GIGYF2 is present in endosomal compartments in the mammalian brains and enhances IGF-1-induced ERK1/2 activation
    • Higashi S, et al. 2010. GIGYF2 is present in endosomal compartments in the mammalian brains and enhances IGF-1-induced ERK1/2 activation. J. Neurochem. 115:423-437.
    • (2010) J. Neurochem , vol.115 , pp. 423-437
    • Higashi, S.1
  • 19
    • 1842427830 scopus 로고    scopus 로고
    • The evolutionary dynamics of eukaryotic gene order
    • Hurst LD, Pal C, Lercher MJ. 2004. The evolutionary dynamics of eukaryotic gene order. Nat. Rev. Genet. 5:299-310.
    • (2004) Nat. Rev. Genet , vol.5 , pp. 299-310
    • Hurst, L.D.1    Pal, C.2    Lercher, M.J.3
  • 20
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV. 2010. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11:113-127.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 21
    • 2942522541 scopus 로고    scopus 로고
    • Characterization of mammalian eIF4E-family members
    • Joshi B, Cameron A, Jagus R. 2004. Characterization of mammalian eIF4E-family members. Eur. J. Biochem. 271:2189-2203.
    • (2004) Eur. J. Biochem , vol.271 , pp. 2189-2203
    • Joshi, B.1    Cameron, A.2    Jagus, R.3
  • 22
    • 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.
    • (2005) BMC Evol. Biol. , vol.5 , pp. 48
    • Joshi, B.1    Lee, K.2    Maeder, D.L.3    Jagus, R.4
  • 23
    • 0034616135 scopus 로고    scopus 로고
    • Functional characterization of five eIF4E isoforms in Caenorhabditis elegans
    • Keiper BD, et al. 2000. Functional characterization of five eIF4E isoforms in Caenorhabditis elegans. J. Biol. Chem. 275:10590-10596.
    • (2000) J. Biol. Chem , vol.275 , pp. 10590-10596
    • Keiper, B.D.1
  • 24
    • 77953633943 scopus 로고    scopus 로고
    • The discovery of zinc fingers and their applications in gene regulation and genome manipulation
    • Klug A. 2010. The discovery of zinc fingers and their applications in gene regulation and genome manipulation. Annu. Rev. Biochem. 79:213-231.
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 213-231
    • Klug, A.1
  • 25
    • 33645036616 scopus 로고    scopus 로고
    • The GYF domain
    • Kofler MM, Freund C. 2006.The GYF domain. FEBS J. 273:245-256.
    • (2006) FEBS J , vol.273 , pp. 245-256
    • Kofler, M.M.1    Freund, C.2
  • 26
    • 77957947158 scopus 로고    scopus 로고
    • ProHits: integrated software for mass spectrometrybased interaction proteomics
    • Liu G, et al. 2010. ProHits: integrated software for mass spectrometrybased interaction proteomics. Nat. Biotechnol. 28:1015-1017.
    • (2010) Nat. Biotechnol , vol.28 , pp. 1015-1017
    • Liu, G.1
  • 27
    • 0033152072 scopus 로고    scopus 로고
    • Capdependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK. 1999. Capdependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell 3:707-716.
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 28
    • 81255191869 scopus 로고    scopus 로고
    • Obesity resistance and increased hepatic expression of catabolism-related mRNAs in Cnot3(+/-) mice
    • Morita M, et al. 2011. Obesity resistance and increased hepatic expression of catabolism-related mRNAs in Cnot3(+/-) mice. EMBO J. 30:4678-4691.
    • (2011) EMBO J , vol.30 , pp. 4678-4691
    • Morita, M.1
  • 29
    • 0346503888 scopus 로고    scopus 로고
    • Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis
    • 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.
    • (2004) Dev. Cell , vol.6 , pp. 69-78
    • Nakamura, A.1    Sato, K.2    Hanyu-Nakamura, K.3
  • 30
    • 0033569387 scopus 로고    scopus 로고
    • The promise of comparative genomics in mammals
    • O'Brien SJ, et al. 1999. The promise of comparative genomics in mammals. Science 286:458-462, 479-481.
    • (1999) Science , vol.286 , pp. 458-462
    • O'Brien, S.J.1
  • 31
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function
    • Pause A, et al. 1994. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature 371:762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1
  • 32
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter JD, Sonenberg N. 2005. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 433:477-480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 33
    • 14444274091 scopus 로고    scopus 로고
    • Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein
    • Rom E, et al. 1998. Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein. J. Biol. Chem. 273:13104-13109.
    • (1998) J. Biol. Chem , vol.273 , pp. 13104-13109
    • Rom, E.1
  • 34
    • 34047174539 scopus 로고    scopus 로고
    • Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms
    • Rosettani P, Knapp S, Vismara MG, Rusconi L, Cameron AD. 2007. Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms. J. Mol. Biol. 368:691-705.
    • (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
  • 35
    • 0036096544 scopus 로고    scopus 로고
    • Paip1 interacts with poly(A) binding protein through two independent binding motifs
    • Roy G, et al. 2002. Paip1 interacts with poly(A) binding protein through two independent binding motifs. Mol. Cell. Biol. 22:3769-3782.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 3769-3782
    • Roy, G.1
  • 36
    • 0032562780 scopus 로고    scopus 로고
    • Identification and characterization of a novel cap-binding protein from Arabidopsis thaliana
    • Ruud KA, Kuhlow C, Goss DJ, Browning KS. 1998. Identification and characterization of a novel cap-binding protein from Arabidopsis thaliana. J. Biol. Chem. 273:10325-10330.
    • (1998) J. Biol. Chem , vol.273 , pp. 10325-10330
    • Ruud, K.A.1    Kuhlow, C.2    Goss, D.J.3    Browning, K.S.4
  • 37
    • 77749323441 scopus 로고    scopus 로고
    • Control of cell survival and proliferation by mammalian eukaryotic initiation factor 4B
    • Shahbazian D, et al. 2010. Control of cell survival and proliferation by mammalian eukaryotic initiation factor 4B. Mol. Cell. Biol. 30:1478-1485.
    • (2010) Mol. Cell. Biol , vol.30 , pp. 1478-1485
    • Shahbazian, D.1
  • 38
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: a software environment for integrated models of biomolecular interaction networks
    • Shannon P, et al. 2003. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13:2498-2504.
    • (2003) Genome Res , vol.13 , pp. 2498-2504
    • Shannon, P.1
  • 39
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. 2009. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136:731-745.
    • (2009) Cell 136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 40
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with elF-4E
    • Stebbins-Boaz B, Cao Q, de Moor CH, Mendez R, Richter JD. 1999. Maskin is a CPEB-associated factor that transiently interacts with elF-4E. Mol. Cell 4:1017-1027.
    • (1999) Mol. Cell , vol.4 , pp. 1017-1027
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.H.3    Mendez, R.4    Richter, J.D.5
  • 41
    • 58249115047 scopus 로고    scopus 로고
    • Interpreting neonatal lethal phenotypes in mouse mutants: insights into gene function and human diseases
    • Turgeon B, Meloche S. 2009. Interpreting neonatal lethal phenotypes in mouse mutants: insights into gene function and human diseases. Physiol. Rev. 89:1-26.
    • (2009) Physiol. Rev , vol.89 , pp. 1-26
    • Turgeon, B.1    Meloche, S.2
  • 42
    • 65249118749 scopus 로고    scopus 로고
    • Cytoplasmic Prep1 interacts with 4EHP inhibiting Hoxb4 translation
    • doi:10.1371/ journal.pone.0005213
    • Villaescusa JC, et al. 2009. Cytoplasmic Prep1 interacts with 4EHP inhibiting Hoxb4 translation. PLoS One 4:e5213. doi:10.1371/ journal.pone.0005213.
    • (2009) PLoS One , vol.4 , pp. 5213
    • Villaescusa, J.C.1
  • 43
    • 25444516785 scopus 로고    scopus 로고
    • Chromosomal clustering of a human transcriptome reveals regulatory background
    • doi:10.1186/1471-2105-6-230
    • Vogel JH, von Heydebreck A, Purmann A, Sperling S. 2005. Chromosomal clustering of a human transcriptome reveals regulatory background. BMC Bioinformatics 6:230. doi:10.1186/1471-2105-6-230.
    • (2005) BMC Bioinformatics , vol.6 , pp. 230
    • Vogel, J.H.1    von Heydebreck, A.2    Purmann, A.3    Sperling, S.4
  • 44
    • 0034730734 scopus 로고    scopus 로고
    • Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5'-cap by domains of eIF4G
    • von der Haar T, Ball PD, McCarthy JE. 2000. Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5'-cap by domains of eIF4G. J. Biol. Chem. 275:30551-30555.
    • (2000) J. Biol. Chem , vol.275 , pp. 30551-30555
    • von der Haar, T.1    Ball, P.D.2    McCarthy, J.E.3
  • 46
    • 62849126891 scopus 로고    scopus 로고
    • Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap
    • Yanagiya A, et al. 2009. Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap. Mol. Cell. Biol. 29:1661-1669.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 1661-1669
    • Yanagiya, A.1
  • 47
    • 34247393290 scopus 로고    scopus 로고
    • Weak binding affinity of human 4EHP for mRNA cap analogs
    • Zuberek J, et al. 2007. Weak binding affinity of human 4EHP for mRNA cap analogs. RNA 13:691-697
    • (2007) RNA , vol.13 , pp. 691-697
    • Zuberek, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.