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Volumn 433, Issue 7025, 2005, Pages 477-480

Regulation of cap-dependent translation by eIF4E inhibitory proteins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CARCINOGENS; CELLS; ENZYME INHIBITION; GROWTH KINETICS; RNA;

EID: 13444259647     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03205     Document Type: Article
Times cited : (794)

References (39)
  • 1
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever, T. Gene-specific regulation by general translation factors. Cell 198, 545-556 (2002).
    • (2002) Cell , vol.198 , pp. 545-556
    • Dever, T.1
  • 2
    • 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., Lee, H., Pause, A. & Sonenberg, N. 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).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 3
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano, J., Gingras, A. C., Sonenberg, N. & Burley, S. K. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89, 951-956 (1997).
    • (1997) Cell , vol.89 , pp. 951-956
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 4
    • 0030826444 scopus 로고    scopus 로고
    • Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein
    • Matsuo, H. et al. Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein. Nature Struct. Biol. 4, 717-724 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 717-724
    • Matsuo, H.1
  • 5
    • 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. 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).
    • (1995) EMBO J. , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 6
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras, A. C., Raught, B. & Sonenberg, N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68, 913-963 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 7
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with eIF-4E
    • Stebbins-Boaz, B., Cao, Q., de Moor, C. H., Mendez, R. & Richter, J. D. Maskin is a CPEB-associated factor that transiently interacts with eIF-4E. Mol. Cell 4, 1017-1027 (1999).
    • (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
  • 8
    • 0037099704 scopus 로고    scopus 로고
    • Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation
    • Cao, Q. & Richter, J. D. Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J. 21, 3852-3862 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3852-3862
    • Cao, Q.1    Richter, J.D.2
  • 9
    • 0036790664 scopus 로고    scopus 로고
    • Bicoid associates with the 5′-cap-bound complex of caudal mRNA and represses translation
    • Niessing, D., Blanke, S. & Jackle, H. Bicoid associates with the 5′-cap-bound complex of caudal mRNA and represses translation. Genes Dev. 16, 2576-2582 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2576-2582
    • Niessing, D.1    Blanke, S.2    Jackle, H.3
  • 10
    • 0346503888 scopus 로고    scopus 로고
    • Drosophila cup is an eIF 4E binding protein that associates with Bruno and regulates oskar MRNA translation in oogenesis
    • Nakamura, A., Sato, K. & Hanyu-Nakamura, K. Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar MRNA translation in oogenesis. Dev. Cell 6, 69-78 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 69-78
    • Nakamura, A.1    Sato, K.2    Hanyu-Nakamura, K.3
  • 11
    • 0346554981 scopus 로고    scopus 로고
    • Cup is an eIF4E binding protein required for both the translational repression of oskarand the recruitment of Barentsz
    • Wilhelm, J. E., Hilton, M., Amos, Q. & Henzel, W. J. Cup is an eIF4E binding protein required for both the translational repression of oskarand the recruitment of Barentsz. J. Cell Biol. 163, 1197-1204 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 1197-1204
    • Wilhelm, J.E.1    Hilton, M.2    Amos, Q.3    Henzel, W.J.4
  • 12
    • 0842328579 scopus 로고    scopus 로고
    • Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression
    • Nelson, M. R., Leidal, A. M. & Smibert, C. A. Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression. EMBO J. 23, 150-159 (2004).
    • (2004) EMBO J. , vol.23 , pp. 150-159
    • Nelson, M.R.1    Leidal, A.M.2    Smibert, C.A.3
  • 13
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas, A., Montine, K. S. & Sonenberg, N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345, 544-547 (1990).
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 14
    • 2942544833 scopus 로고    scopus 로고
    • Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells
    • Avdulov, S. et al. Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells. Cancer Cell 5, 553-563 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 553-563
    • Avdulov, S.1
  • 15
    • 2442648845 scopus 로고    scopus 로고
    • The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
    • Ruggero, D. et al. The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nature Med. 10, 484-486 (2004).
    • (2004) Nature Med. , vol.10 , pp. 484-486
    • Ruggero, D.1
  • 16
    • 1642586272 scopus 로고    scopus 로고
    • Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy
    • Wendel, H. G. et al. Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 428, 332-337 (2004).
    • (2004) Nature , vol.428 , pp. 332-337
    • Wendel, H.G.1
  • 17
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero, D. & Pandolfi, P. P. Does the ribosome translate cancer? Nature Rev. Cancer 3, 179-192 (2003).
    • (2003) Nature Rev. Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 18
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau, D., Gingras, A. C., Pause, A. & Sonenberg, N. The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 13, 2415-2420 (1996).
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 19
    • 0344063370 scopus 로고    scopus 로고
    • Will mTOR inhibitors make it as cancer drugs?
    • Sawyers, C. L. Will mTOR inhibitors make it as cancer drugs? Cancer Cell 4, 343-384 (2003).
    • (2003) Cancer Cell , vol.4 , pp. 343-384
    • Sawyers, C.L.1
  • 20
    • 0023124676 scopus 로고
    • Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F
    • Duncan, R., Milburn, S. C. & Hershey, J. W. Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F. J. Biol. Chem. 262, 380-383 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 380-383
    • Duncan, R.1    Milburn, S.C.2    Hershey, J.W.3
  • 21
    • 0030009739 scopus 로고    scopus 로고
    • A reevaluation of the cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate
    • Rau, M., Ohlmann, T., Morley, S. J. & Pain, V. M. A reevaluation of the cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate. J. Biol. Chem. 271, 8983-8990 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8983-8990
    • Rau, M.1    Ohlmann, T.2    Morley, S.J.3    Pain, V.M.4
  • 22
    • 0027445185 scopus 로고
    • Translation factors are effectors of cell growth and tumorigenesis
    • Sonenberg, N. Translation factors are effectors of cell growth and tumorigenesis. Curr. Opin. Cell Biol. 5, 955-960 (1993).
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 955-960
    • Sonenberg, N.1
  • 23
    • 0026723117 scopus 로고
    • mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E
    • Koromilas, A. E., Lazaris-Karatzas, A. & Sonenberg, N. mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. EMBO J. 11, 4153-4158 (1992).
    • (1992) EMBO J. , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 24
    • 0037273324 scopus 로고    scopus 로고
    • Translational control and metastatic progression: Enhanced activity of the mRNA cap-binding protein eIF-4E selectively enhances translation of metastasis-related mRNAs
    • Graff, J. R. & Zimmer, S. G. Translational control and metastatic progression: enhanced activity of the mRNA cap-binding protein eIF-4E selectively enhances translation of metastasis-related mRNAs. Clin. Exp. Metastasis 20, 265-273 (2003).
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 265-273
    • Graff, J.R.1    Zimmer, S.G.2
  • 26
    • 0034927379 scopus 로고    scopus 로고
    • Protein synthesis at synaptic sites on dendrites
    • Steward, O. & Schuman, E. M. Protein synthesis at synaptic sites on dendrites. Annu. Rev. Neurosci. 24, 299-325 (2001).
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 299-325
    • Steward, O.1    Schuman, E.M.2
  • 27
    • 0036605990 scopus 로고    scopus 로고
    • Selective translation of mRNAs at synapses
    • Richter, J. D. & Lorenz, L. J. Selective translation of mRNAs at synapses. Curr. Opin. Neurobiol. 12, 300-304 (2002).
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 300-304
    • Richter, J.D.1    Lorenz, L.J.2
  • 28
    • 0032692620 scopus 로고    scopus 로고
    • A transient, neuron-wide form of CREB-mediated long-term facilitation can be stabilized at specific synapses by local protein synthesis
    • Cassadio, A. et al. A transient, neuron-wide form of CREB-mediated long-term facilitation can be stabilized at specific synapses by local protein synthesis. Cell 99, 221-237 (1999).
    • (1999) Cell , vol.99 , pp. 221-237
    • Cassadio, A.1
  • 29
    • 1342322145 scopus 로고    scopus 로고
    • Translational control by MAPK signaling in long-term synaptic plasticity and memory
    • Kelleher, R. J., Govindarajan, A., Jung, H., Kang, H. & Tonegawa, S. Translational control by MAPK signaling in long-term synaptic plasticity and memory. Cell 116, 467-479 (2004).
    • (2004) Cell , vol.116 , pp. 467-479
    • Kelleher, R.J.1    Govindarajan, A.2    Jung, H.3    Kang, H.4    Tonegawa, S.5
  • 30
    • 0037039358 scopus 로고    scopus 로고
    • A rapamycin-sensitive signaling pathway contributes to long-term synaptic plasticity in the hippocampus
    • Tang, S. J. et al. A rapamycin-sensitive signaling pathway contributes to long-term synaptic plasticity in the hippocampus. Proc. Natl Acad. Sci. USA 99, 467-472 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 467-472
    • Tang, S.J.1
  • 31
    • 2542542866 scopus 로고    scopus 로고
    • Selective modulation of some forms of Schaffer collateral-CA1 synaptic plasticity in inice with a disruption of the CPEB-1 gene
    • Alarcon, J. M. et al. Selective modulation of some forms of Schaffer collateral-CA1 synaptic plasticity in inice with a disruption of the CPEB-1 gene. Learn. Mem. 11, 318-327 (2004).
    • (2004) Learn. Mem. , vol.11 , pp. 318-327
    • Alarcon, J.M.1
  • 32
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses
    • Wu, L. et al. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses. Neuron 21, 1129-1139 (1998).
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1
  • 33
    • 0036565678 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses
    • Huang, Y. S., Jung, M. Y., Sarkissian, M. & Richter, J. D. N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses. EMBO J. 21, 2139-2148 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2139-2148
    • Huang, Y.S.1    Jung, M.Y.2    Sarkissian, M.3    Richter, J.D.4
  • 34
    • 0035924590 scopus 로고    scopus 로고
    • Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation
    • Campbell, D. S. & Holt, C. E. Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation. Neuron 32, 1013-1026 (2001).
    • (2001) Neuron , vol.32 , pp. 1013-1026
    • Campbell, D.S.1    Holt, C.E.2
  • 35
    • 0035881727 scopus 로고    scopus 로고
    • Suppression of cap-dependent translation in mitosis
    • Pyronnet, S., Dostie, J. & Sonenberg, N. Suppression of cap-dependent translation in mitosis. Genes Dev. 15, 2083-2093 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2083-2093
    • Pyronnet, S.1    Dostie, J.2    Sonenberg, N.3
  • 36
    • 0035806992 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of the translational repressor eIF-4E binding protein-1 (4E-BP1)
    • Heesom, K. J., Gampel, A., Mellor, H. & Denton, R. M. Cell cycle-dependent phosphorylation of the translational repressor eIF-4E binding protein-1 (4E-BP1). Curr. Biol. 11, 1374-1379 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1374-1379
    • Heesom, K.J.1    Gampel, A.2    Mellor, H.3    Denton, R.M.4
  • 37
    • 0034770191 scopus 로고    scopus 로고
    • Adipose tissue reduction in mice lacking the translational inhibitor 4E-BPI
    • Tsukiyama-Kohara, K. et al. Adipose tissue reduction in mice lacking the translational inhibitor 4E-BPI. Nature Med. 7, 1128-1132 (2001).
    • (2001) Nature Med. , vol.7 , pp. 1128-1132
    • Tsukiyama-Kohara, K.1
  • 38
    • 0037415692 scopus 로고    scopus 로고
    • The proline-rich homeodomain protein, PRH, is a tissue-specific inhibitor of eIF4E-dependent cyclin D1 mRNA transport and growth
    • Topisirovic, I. et al. The proline-rich homeodomain protein, PRH, is a tissue-specific inhibitor of eIF4E-dependent cyclin D1 mRNA transport and growth. EMBO J. 22, 689-703 (2003).
    • (2003) EMBO J. , vol.22 , pp. 689-703
    • Topisirovic, I.1
  • 39
    • 3242704789 scopus 로고    scopus 로고
    • Emx2 homeodomain transcription factor interacts with eukaryotic translation initiation factor 4E (eIF4E) in the axons of olfactory sensory neurons
    • Nedelec, S. et al. Emx2 homeodomain transcription factor interacts with eukaryotic translation initiation factor 4E (eIF4E) in the axons of olfactory sensory neurons. Proc. Natl Acad. Sci. USA 101, 10815-10820 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10815-10820
    • Nedelec, S.1


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