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Volumn 24, Issue 11, 2004, Pages 4920-4928

Selective modification of eukaryotic initiation factor 4F (eIF4F) at the onset of cell differentiation: Recruitment of eIF4GII and long-lasting phosphorylation of eIF4E

Author keywords

[No Author keywords available]

Indexed keywords

CAPPED RNA; CYTOKINE; INITIATION FACTOR 4E; INITIATION FACTOR 4F; INITIATION FACTOR 4G; INITIATION FACTOR 4G2; MESSENGER RNA; POLYADENYLIC ACID; THROMBOPOIETIN; UNCLASSIFIED DRUG;

EID: 2442679170     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.11.4920-4928.2004     Document Type: Article
Times cited : (39)

References (51)
  • 2
    • 0030774558 scopus 로고    scopus 로고
    • Thrombopoietin-induced expression of the glycoprotein IIb gene involves the transcription factor PU.1/Spi-1 in UT7-Mpl cells
    • Doubeikovski, A., G. Uzan, Z. Doubeikovski, M. H. Prandini, F. Porteu, S. Gisselbrecht, and I. Dusanter-Fourt. 1997. Thrombopoietin-induced expression of the glycoprotein IIb gene involves the transcription factor PU.1/Spi-1 in UT7-Mpl cells. J. Biol. Chem. 272:24300-24307.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24300-24307
    • Doubeikovski, A.1    Uzan, G.2    Doubeikovski, Z.3    Prandini, M.H.4    Porteu, F.5    Gisselbrecht, S.6    Dusanter-Fourt, I.7
  • 3
    • 0033568190 scopus 로고    scopus 로고
    • Cellular stress in xenopus kidney cells enhances the phosphorylation of eukaryotic translation initiation factor (eIF)4E and the association of eIF4F with poly(A)-binding protein
    • Fraser, C. S., V. M. Pain, and S. J. Morley. 1999. Cellular stress in xenopus kidney cells enhances the phosphorylation of eukaryotic translation initiation factor (eIF)4E and the association of eIF4F with poly(A)-binding protein. Biochem. J. 342:519-526.
    • (1999) Biochem. J. , vol.342 , pp. 519-526
    • Fraser, C.S.1    Pain, V.M.2    Morley, S.J.3
  • 4
    • 0035282971 scopus 로고    scopus 로고
    • A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements
    • Gao, M., C. J. Wilusz, S. W. Peltz, and J. Wilusz. 2001. A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J. 20:1134-1143.
    • (2001) EMBO J. , vol.20 , pp. 1134-1143
    • Gao, M.1    Wilusz, C.J.2    Peltz, S.W.3    Wilusz, J.4
  • 5
    • 0035076221 scopus 로고    scopus 로고
    • Thrombopoietin-mediated sustained activation of extracellular signal-regulated kinase in UT7-Mpl cells requires both Ras-Raf-1- and Rap1-B-Raf-dependent pathways
    • Garcia, J., J. de Gunzburg, A. Eychene, S. Gisselbrecht, and F. Porteu. 2001. Thrombopoietin-mediated sustained activation of extracellular signal-regulated kinase in UT7-Mpl cells requires both Ras-Raf-1- and Rap1-B-Raf-dependent pathways. Mol. Cell. Biol. 21:2659-2670.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2659-2670
    • Garcia, J.1    De Gunzburg, J.2    Eychene, A.3    Gisselbrecht, S.4    Porteu, F.5
  • 6
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras, A. C., B. Raught, and N. Sonenberg. 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
  • 7
    • 0027219266 scopus 로고
    • TIF4631 and TIF4632: Two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function
    • Goyer, C., M. Altmann, H. S. Lee, A. Blanc, M. Deshmukh, J. L. Woolford, Jr., H. Trachsel, and N. Sonenberg. 1993. TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function. Mol. Cell. Biol. 13:4860-4874.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4860-4874
    • Goyer, C.1    Altmann, M.2    Lee, H.S.3    Blanc, A.4    Deshmukh, M.5    Woolford Jr., J.L.6    Trachsel, H.7    Sonenberg, N.8
  • 9
    • 0034282752 scopus 로고    scopus 로고
    • Multiple portions of poly(A)-binding protein stimulate translation in vivo
    • Gray, N. K., J. M. Coller, K. S. Dickson, and M. Wickens. 2000. Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 19:4723-4733.
    • (2000) EMBO J. , vol.19 , pp. 4723-4733
    • Gray, N.K.1    Coller, J.M.2    Dickson, K.S.3    Wickens, M.4
  • 10
    • 0033559137 scopus 로고    scopus 로고
    • Differential regulation of 4E-BP1 and 4E-BP2, two repressors of translation initiation, during human myeloid cell differentiation
    • Grolleau, A., N. Sonenberg, J. Wietzerbin, and L. Beretta. 1999. Differential regulation of 4E-BP1 and 4E-BP2, two repressors of translation initiation, during human myeloid cell differentiation. J. Immunol. 162:3491-3497.
    • (1999) J. Immunol. , vol.162 , pp. 3491-3497
    • Grolleau, A.1    Sonenberg, N.2    Wietzerbin, J.3    Beretta, L.4
  • 11
    • 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., S. Mader, A. Pause, and N. Sonenberg. 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
  • 12
    • 0030832026 scopus 로고    scopus 로고
    • eIF4G dramatically enhances the binding of eIF4E to the mRNA 5′-cap structure
    • Haghighat, A., and N. Sonenberg. 1997. eIF4G dramatically enhances the binding of eIF4E to the mRNA 5′-cap structure. J. Biol. Chem. 272:21677-21680.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2
  • 13
    • 0029861190 scopus 로고    scopus 로고
    • The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase
    • Haghighat, A., Y. Svitkin, I. Novoa, E. Kuechler, T. Skern, and N. Sonenberg. 1996. The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase. J. Virol. 70:8444-8450.
    • (1996) J. Virol. , vol.70 , pp. 8444-8450
    • Haghighat, A.1    Svitkin, Y.2    Novoa, I.3    Kuechler, E.4    Skern, T.5    Sonenberg, N.6
  • 14
    • 0041589832 scopus 로고    scopus 로고
    • The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection
    • He, H., T. von der Haar, C. R. Singh, M. Ii, B. Li, A. G. Hinnebusch, J. E. McCarthy, and K. Asano. 2003. The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection. Mol. Cell. Biol. 23:5431-5445.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5431-5445
    • He, H.1    Von Der Haar, T.2    Singh, C.R.3    Ii, M.4    Li, B.5    Hinnebusch, A.G.6    McCarthy, J.E.7    Asano, K.8
  • 15
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataka, H., A. Gradi, and N. Sonenberg. 1998. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17:7480-7489.
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 16
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka, H., and N. Sonenberg. 1997. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell. Biol. 17:6940-6947.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 17
    • 0033027161 scopus 로고    scopus 로고
    • Thrombopoietin and hematopoietic stem cell development
    • Kaushansky, K. 1999. Thrombopoietin and hematopoietic stem cell development. Ann. N. Y. Acad. Sci. 872:314-319.
    • (1999) Ann. N. Y. Acad. Sci. , vol.872 , pp. 314-319
    • Kaushansky, K.1
  • 18
    • 0026034133 scopus 로고
    • Establishment and characterization of a human leukemic cell line with megakaryocytic features: Dependency on granulocyte-macrophage colony-stimulating factor, interleukin 3, or erythropoietin for growth and survival
    • Komatsu, N., H. Nakauchi, A. Miwa, T. Ishihara, M. Eguchi, M. Moroi, M. Okada, Y. Sato, H. Wada, Y. Yawata, et al. 1991. Establishment and characterization of a human leukemic cell line with megakaryocytic features: dependency on granulocyte-macrophage colony-stimulating factor, interleukin 3, or erythropoietin for growth and survival. Cancer Res. 51:341-348.
    • (1991) Cancer Res. , vol.51 , pp. 341-348
    • Komatsu, N.1    Nakauchi, H.2    Miwa, A.3    Ishihara, T.4    Eguchi, M.5    Moroi, M.6    Okada, M.7    Sato, Y.8    Wada, H.9    Yawata, Y.10
  • 19
    • 0036178103 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth
    • Lachance, P. E., M. Miron, B. Raught, N. Sonenberg, and P. Lasko. 2002. Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth. Mol. Cell. Biol. 22:1656-1663.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1656-1663
    • Lachance, P.E.1    Miron, M.2    Raught, B.3    Sonenberg, N.4    Lasko, P.5
  • 20
    • 0030883848 scopus 로고    scopus 로고
    • PHAS/4E-BPs as regulators of mRNA translation and cell proliferation
    • Lawrence, J. C., Jr., and R. T. Abraham. 1997. PHAS/4E-BPs as regulators of mRNA translation and cell proliferation. Trends Biochem. Sci. 22:345-349.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 345-349
    • Lawrence Jr., J.C.1    Abraham, R.T.2
  • 21
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas, A., K. S. Montine, and N. Sonenberg. 1990. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345:544-547.
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 22
    • 0033852315 scopus 로고    scopus 로고
    • Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation
    • Lomakin, I. B., C. U. Hellen, and T. V. Pestova. 2000. Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation. Mol. Cell. Biol. 20:6019-6029.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6019-6029
    • Lomakin, I.B.1    Hellen, C.U.2    Pestova, T.V.3
  • 23
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressors 4E-binding proteins
    • Mader, S., H. Lee, A. Pause, and N. Sonenberg. 1995. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15:4990-4997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 24
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano, J., A. C. Gingras, N. Sonenberg, and S. K. Burley. 1997. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89:951-961.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 25
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich, W. B., M. L. Balasta, D. J. Goss, and R. E. Rhoads. 1994. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. USA 91:7668-7672.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 26
    • 0030610901 scopus 로고    scopus 로고
    • eIF4G: Translation's mystery factor begins to yield its secrets
    • Morley, S. J., P. S. Curtis, and V. M. Pain. 1997. eIF4G: translation's mystery factor begins to yield its secrets. RNA 3:1085-1104.
    • (1997) RNA , vol.3 , pp. 1085-1104
    • Morley, S.J.1    Curtis, P.S.2    Pain, V.M.3
  • 27
    • 0037031845 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor (eIF) 4E is not required for de novo protein synthesis following recovery from hypertonic stress in human kidney cells
    • Morley, S. J., and S. Naegele. 2002. Phosphorylation of eukaryotic initiation factor (eIF) 4E is not required for de novo protein synthesis following recovery from hypertonic stress in human kidney cells. J. Biol. Chem. 277:32855-32859.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32855-32859
    • Morley, S.J.1    Naegele, S.2
  • 28
    • 0031054338 scopus 로고    scopus 로고
    • The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate
    • Ohlmann, T., V. M. Pain, W. Wood, M. Rau, and S. J. Morley. 1997. The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate. EMBO J. 16:844-855.
    • (1997) EMBO J. , vol.16 , pp. 844-855
    • Ohlmann, T.1    Pain, V.M.2    Wood, W.3    Rau, M.4    Morley, S.J.5
  • 29
    • 0036308653 scopus 로고    scopus 로고
    • In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system
    • Ohlmann, T., D. Prevot, D. Decimo, F. Roux, J. Garin, S. J. Morley, and J. L. Darlix. 2002. In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system. J. Mol. Biol. 318:9-20.
    • (2002) J. Mol. Biol. , vol.318 , pp. 9-20
    • Ohlmann, T.1    Prevot, D.2    Decimo, D.3    Roux, F.4    Garin, J.5    Morley, S.J.6    Darlix, J.L.7
  • 30
    • 0033153302 scopus 로고    scopus 로고
    • The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms
    • Otero, L. J., M. P. Ashe, and A. B. Sachs. 1999. The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. EMBO J. 18:3153-3163.
    • (1999) EMBO J. , vol.18 , pp. 3153-3163
    • Otero, L.J.1    Ashe, M.P.2    Sachs, A.B.3
  • 31
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain, V. M. 1996. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236:747-771.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 32
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., G. J. Belsham, A. C. Gingras, O. Donze, T. A. Lin, J. C. Lawrence, Jr., and N. Sonenberg. 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    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 33
    • 0029963565 scopus 로고    scopus 로고
    • Functional regions of the mouse thrombopoietin receptor cytoplasmic domain: Evidence for a critical region which is involved in differentiation and can be complemented by erythropoietin
    • Porteu, F., M. C. Rouyez, L. Cocault, L. Benit, M. Charon, F. Picard, S. Gisselbrecht, M. Souyri, and I. Dusanter-Fourt. 1996. Functional regions of the mouse thrombopoietin receptor cytoplasmic domain: evidence for a critical region which is involved in differentiation and can be complemented by erythropoietin. Mol. Cell. Biol. 16:2473-2482.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2473-2482
    • Porteu, F.1    Rouyez, M.C.2    Cocault, L.3    Benit, L.4    Charon, M.5    Picard, F.6    Gisselbrecht, S.7    Souyri, M.8    Dusanter-Fourt, I.9
  • 34
    • 0032577691 scopus 로고    scopus 로고
    • 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family
    • Poulin, F., A. C. Gingras, H. Olsen, S. Chevalier, and N. Sonenberg. 1998. 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family. J. Biol. Chem. 273:14002-14007.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14002-14007
    • Poulin, F.1    Gingras, A.C.2    Olsen, H.3    Chevalier, S.4    Sonenberg, N.5
  • 35
    • 0032473954 scopus 로고    scopus 로고
    • Dual function of the messenger RNA cap structure in poly(A) -tail-promoted translation in yeast
    • Preiss, T., and M. W. Hentze. 1998. Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast. Nature 392:516-520.
    • (1998) Nature , vol.392 , pp. 516-520
    • Preiss, T.1    Hentze, M.W.2
  • 36
    • 0032858414 scopus 로고    scopus 로고
    • From factors to mechanisms: Translation and translational control in eukaryctes
    • Preiss, T., and M. W. Hentze. 1999. From factors to mechanisms: translation and translational control in eukaryctes. Curr. Opin. Genet. Dev. 9:515-521.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 515-521
    • Preiss, T.1    Hentze, M.W.2
  • 37
    • 0037781584 scopus 로고    scopus 로고
    • Conducting the initiation of protein synthesis: The role of eIF4G
    • Prevot, D., J. L. Darlix, and T. Ohlmann, 2003. Conducting the initiation of protein synthesis: the role of eIF4G. Biol. Cell 95:141-156.
    • (2003) Biol. Cell , vol.95 , pp. 141-156
    • Prevot, D.1    Darlix, J.L.2    Ohlmann, T.3
  • 38
    • 0345373936 scopus 로고    scopus 로고
    • Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning
    • Prevot, D., D. Decimo, C. H. Herbreteau, F. Roux, J. Garin, J. L. Darlix, and T. Ohlmann. 2003. Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning. EMBO J. 22:1909-1921.
    • (2003) EMBO J. , vol.22 , pp. 1909-1921
    • Prevot, D.1    Decimo, D.2    Herbreteau, C.H.3    Roux, F.4    Garin, J.5    Darlix, J.L.6    Ohlmann, T.7
  • 39
    • 0030666262 scopus 로고    scopus 로고
    • Molecular mechanisms for the control of translation by insulin
    • Proud, C. G., and R. M. Denton. 1997. Molecular mechanisms for the control of translation by insulin. Biochem. J. 328:329-341.
    • (1997) Biochem. J. , vol.328 , pp. 329-341
    • Proud, C.G.1    Denton, R.M.2
  • 40
    • 0035881727 scopus 로고    scopus 로고
    • Suppression of cap-dependent translation in mitosis
    • Pyronnet, S., J. Dostie, and N. Sonenberg. 2001. Suppression of cap-dependent translation in mitosis. Genes Dev. 15:2083-2093.
    • (2001) Genes Dev. , vol.15 , pp. 2083-2093
    • Pyronnet, S.1    Dostie, J.2    Sonenberg, N.3
  • 41
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E
    • Pyronnet, S., H. Imataka, A. C. Gingras, R. Fukunaga, T. Hunter, and N. Sonenberg. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J. 18:270-279.
    • (1999) EMBO J. , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 42
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • Raught, B., A. C. Gingras, S. P. Gygi, H. Imataka, S. Morino, A. Gradi, R. Aebersold, and N. Sonenberg. 2000. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19:434-444.
    • (2000) EMBO J. , vol.19 , pp. 434-444
    • Raught, B.1    Gingras, A.C.2    Gygi, S.P.3    Imataka, H.4    Morino, S.5    Gradi, A.6    Aebersold, R.7    Sonenberg, N.8
  • 43
    • 0036479313 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA
    • Scheper, G. C., B. van Kollenburg, J. Hu, Y. Luo, D. J. Goss, and C. G. Proud. 2002. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem. 277:3303-3309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3303-3309
    • Scheper, G.C.1    Van Kollenburg, B.2    Hu, J.3    Luo, Y.4    Goss, D.J.5    Proud, C.G.6
  • 45
    • 0032054816 scopus 로고    scopus 로고
    • The mRNA 5′ cap-binding protein eIF4E and control of cell growth
    • Sonenberg, N., and A. C. Gingras. 1998. The mRNA 5′ cap-binding protein eIF4E and control of cell growth. Curr. Opin. Cell Biol. 10:268-275.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 268-275
    • Sonenberg, N.1    Gingras, A.C.2
  • 46
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G
    • Tarun, S. Z., Jr., and A. B. Sachs. 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15:7168-7177.
    • (1996) EMBO J. , vol.15 , pp. 7168-7177
    • Tarun Jr., S.Z.1    Sachs, A.B.2
  • 47
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun, S. Z., Jr., and A. B. Sachs. 1995. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9:2997-3007.
    • (1995) Genes Dev. , vol.9 , pp. 2997-3007
    • Tarun Jr., S.Z.1    Sachs, A.B.2
  • 48
    • 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., P. D. BaII, and J. E. McCarthy. 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    Baii, P.D.2    McCarthy, J.E.3
  • 49
    • 0032540244 scopus 로고
    • The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways
    • Wang, X., A. Flynn, A. J. Waskiewicz, B. L. Webb, R. G. Vries, I. A. Baines, J. A. Cooper, and C. G. Proud. 1993. The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways. J. Biol. Chem. 273:9373-9377.
    • (1993) J. Biol. Chem. , vol.273 , pp. 9373-9377
    • Wang, X.1    Flynn, A.2    Waskiewicz, A.J.3    Webb, B.L.4    Vries, R.G.5    Baines, I.A.6    Cooper, J.A.7    Proud, C.G.8
  • 50
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz, A. J., J. C. Johnson, B. Penn, M. Mahalingam, S. R. Kimball, and J. A. Cooper. 1999. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell. Biol. 19:1871-1880.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimball, S.R.5    Cooper, J.A.6
  • 51
    • 0030011629 scopus 로고    scopus 로고
    • Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins
    • Whalen, S. G., A. C. Gingras, L. Amankwa, S. Mader, P. E. Branton, R. Aebersold, and N. Sonenberg. 1996. Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins. J. Biol. Chem. 271:11831-11837.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11831-11837
    • Whalen, S.G.1    Gingras, A.C.2    Amankwa, L.3    Mader, S.4    Branton, P.E.5    Aebersold, R.6    Sonenberg, N.7


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