Cited by 520RNA and protein synthesis mechanismsPI3K/AKT/mTOR signaling in cancerRNA Research and Splicing

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Signalling to translation: how signal transduction pathways control the protein synthetic machinery

Proud, Christopher G.·2007·Biochemical Journal

DOI 10.1042/bj20070024

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Abstract

Recent advances in our understanding of both the regulation of components of the translational machinery and the upstream signalling pathways that modulate them have provided important new insights into the mechanisms by which hormones, growth factors, nutrients and cellular energy status control protein synthesis in mammalian cells. The importance of proper control of mRNA translation is strikingly illustrated by the fact that defects in this process or its control are implicated in a number of disease states, such as cancer, tissue hypertrophy and neurodegeneration. Signalling pathways such as those involving mTOR (mammalian target of rapamycin) and mitogen-activated protein kinases modulate the phosphorylation of translation factors, the activities of the protein kinases that act upon them and the association of RNA-binding proteins with specific mRNAs. These effects contribute both to the overall control of protein synthesis (which is linked to cell growth) and to the modulation of the translation or stability of specific mRNAs. However, important questions remain about both the contributions of individual regulatory events to the control of general protein synthesis and the mechanisms by which the translation of specific mRNAs is controlled.

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Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
ERK and p38 MAPK-Activated Protein Kinases: a Family of Protein Kinases with Diverse Biological Functions
Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540
Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB
Sarbassov, D. D., Ali, S. M., Sengupta, S., Sheen, J.-H., Hsu, P. P., Bagley, A. F., Markhard, A. L., & Sabatini, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.029 · Cited by 2,365
eIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
Gingras, A., Raught, B., & Sonenberg, N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.913 · Cited by 2,103
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097
Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677
Growing roles for the mTOR pathway
Sarbassov, D. D., Ali, S. M., & Sabatini, D. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.09.009 · Cited by 1,590
The renaissance of GSK3
Cohen, P., & Frame, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096075 · Cited by 1,493
SIN1/MIP1 Maintains rictor-mTOR Complex Integrity and Regulates Akt Phosphorylation and Substrate Specificity
Jacinto, E., Facchinetti, V., Liu, D., Soto, N., Wei, S., Jung, S. Y., Huang, Q., Qin, J., & Su, B. (2006) · Cell · doi:10.1016/j.cell.2006.08.033 · Cited by 1,407
Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex
Brugarolas, J., Lei, K., Hurley, R. L., Manning, B. D., Reiling, J. H., Hafen, E., Witters, L. A., Ellisen, L. W., & Kaelin, W. G. (2004) · Genes & Development · doi:10.1101/gad.1256804 · Cited by 1,384
TSC2 Integrates Wnt and Energy Signals via a Coordinated Phosphorylation by AMPK and GSK3 to Regulate Cell Growth
Inoki, K., Ouyang, H., Zhu, T., Lindvall, C., Wang, Y., Zhang, X., Yang, Q., Bennett, C., Harada, Y., Stankunas, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.055 · Cited by 1,377
Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis
Scheuner, D. L., Song, B., McEwen, E. L., Liu, C., Laybutt, D. R., Gillespie, P. J., Saunders, T. L., Bonner‐Weir, S., & Kaufman, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00265-9 · Cited by 1,355
Regulation of 4E-BP1 phosphorylation: a novel two-step mechanismPreprint
Gingras, A., Gygi, S. P., Raught, B., Polakiewicz, R. D., Abraham, R. T., Hoekstra, M. F., Aebersold, R. H., & Sonenberg, N. (1999) · Genes & Development · doi:10.1101/gad.13.11.1422 · Cited by 1,348
Impaired On/Off Regulation of TNF Biosynthesis in Mice Lacking TNF AU-Rich Elements
Kontoyiannis, D. L., Pasparakis, M., Pizarro, T. T., Cominelli, F., & Kollias, G. A. (1999) · Immunity · doi:10.1016/s1074-7613(00)80038-2 · Cited by 1,329
Perturbations of the AKT signaling pathway in human cancer
Altomare, D. A., & Testa, J. R. (2005) · Oncogene · doi:10.1038/sj.onc.1209085 · Cited by 1,326
mTOR and cancer: insights into a complex relationship
Sabatini, D. M. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1974 · Cited by 1,322
Phosphorylation and Functional Inactivation of TSC2 by Erk
Ma, L., Chen, Z., Erdjument-Bromage, H., Tempst, P., & Pandolfi, P. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.031 · Cited by 1,268
Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis
Cully, M., You, H., Levine, A. J., & Mak, T. W. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1819 · Cited by 1,267
mTOR and S6K1 Mediate Assembly of the Translation Preinitiation Complex through Dynamic Protein Interchange and Ordered Phosphorylation Events
Holz, M. K., Ballif, B. A., Gygi, S. P., & Blenis, J. (2005) · Cell · doi:10.1016/j.cell.2005.10.024 · Cited by 1,262
Translational control of gene expression
Hannig, E. M. (2001) · BioEssays · doi:10.1002/bies.1108 · Cited by 1,194
RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1
Burnett, P. E., Barrow, R. K., Cohen, N. A., Snyder, S. H., & Sabatini, D. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1432 · Cited by 1,130
The TSC1-2 tumor suppressor controls insulin–PI3K signaling via regulation of IRS proteins
Harrington, L. S., Findlay, G. M., Gray, A., Толкачева, Т. А., Wigfield, S., Rebholz, H., Barnett, J., Leslie, N. R., Cheng, S., Shepherd, P. R., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403069 · Cited by 1,123
Rheb Binds and Regulates the mTOR Kinase
Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., & Avruch, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.053 · Cited by 1,005
RNA granules
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984
Dysregulation of the TSC-mTOR pathway in human disease
Inoki, K., Corradetti, M. N., & Guan, K. (2004) · Nature Genetics · doi:10.1038/ng1494 · Cited by 980
Mammalian TOR: a homeostatic ATP sensor
Dennis, P. B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S. C., & Thomas, G. (2001) · Science · doi:10.1126/science.1063518 · Cited by 962
Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy
Wendel, H., de Stanchina, E., Fridman, J. S., Malina, A., Ray, S., Kogan, S. C., Cordon‐Cardo, C., Pelletier, J., & Lowe, S. W. (2004) · Nature · doi:10.1038/nature02369 · Cited by 956
Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
Waskiewicz, A. J., Flynn, A., Proud, C. G., & Cooper, J. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1909 · Cited by 951
AU-rich elements and associated factors: are there unifying principles?
Barreau, C. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki1012 · Cited by 907
Management of cellular energy by the AMP‐activated protein kinase system
Hardie, D. G., Scott, J. W., Pan, D. A., & Hudson, E. R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00560-x · Cited by 868
Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase
Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862
Phosphorylation of the Translational Repressor PHAS-I by the Mammalian Target of Rapamycin
Brunn, G. J., Hudson, C. C., Sekulić, A., Williams, J. M., Hosoi, H., Houghton, P. J., Lawrence, J. C., & Abraham, R. T. (1997) · Science · doi:10.1126/science.277.5322.99 · Cited by 846
Advances in protein kinase B signalling: AKTion on multiple fronts
Brazil, D. P., Yang, Z., & Hemmings, B. A. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.03.006 · Cited by 840
Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling
Tee, A. R., Fingar, D. C., Manning, B. D., Kwiatkowski, D. J., Cantley, L. C., & Blenis, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202476899 · Cited by 827
GSK3 inhibitors: development and therapeutic potential
Cohen, P., & Goedert, M. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1415 · Cited by 801
Drosophila S6 kinase: a regulator of cell size.
Montagne, J., Stewart, M. J., Stocker, H., Hafen, E., Kozma, S., & Thomas, G. (1999) · Science · doi:10.1126/science.285.5436.2126 · Cited by 785
S6K1 −/− / S6K2 −/− Mice Exhibit Perinatal Lethality and Rapamycin-Sensitive 5′-Terminal Oligopyrimidine mRNA Translation and Reveal a Mitogen-Activated Protein Kinase-Dependent S6 Kinase Pathway
Pende, M., Um, S. H., Mieulet, V., Sticker, M., Goss, V. L., Mestan, J., Mueller, M., Fumagalli, S., Kozma, S. C., & Thomas, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3112-3124.2004 · Cited by 766
MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis
Kotlyarov, A., Neininger, A., Schubert, C., Eckert, R., Birchmeier, C., Volk, H.-D., & Gaestel, M. (1999) · Nature Cell Biology · doi:10.1038/10061 · Cited by 763
ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth
Bi, M., Naczki, C., Koritzinsky, M., Fels, D. R., Blais, J. D., Hu, N., Harding, H. P., Novoa, I., Varia, M. A., Raleigh, J. A., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600777 · Cited by 756
Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
Roux, P. P., Ballif, B. A., Anjum, R., Gygi, S. P., & Blenis, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405659101 · Cited by 750
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. B., Pause, A., & Sonenberg, N. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.9.4990 · Cited by 685
The Mammalian Target of Rapamycin (mTOR) Partner, Raptor, Binds the mTOR Substrates p70 S6 Kinase and 4E-BP1 through Their TOR Signaling (TOS) Motif
Nojima, H., Tokunaga, C., Eguchi, S., Oshiro, N., Sujuti, H., Yoshino, K., Hara, K., Tanaka, N., Avruch, J., & Yonezawa, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200665200 · Cited by 678
Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasisPreprint
Ruvinsky, I., Sharon, N., Lerer, T., Cohen, H., Stolovich-Rain, M., Nir, T., Dor, Y., Zisman, P., & Meyuhas, O. (2005) · Genes & Development · doi:10.1101/gad.351605 · Cited by 668
MNK1, a new MAP kinase‐activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
Fukunaga, R., & Hunter, T. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1921 · Cited by 666
Translational control in biology and medicine
Mathews, M. B., Sonenberg, N., & Hershey, J. W. B. (2007) · Cited by 661
mTOR·RICTOR Is the Ser473 Kinase for Akt/Protein Kinase B in 3T3-L1 Adipocytes
Hresko, R. C., & Mueckler, M. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508361200 · Cited by 642
Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E
Pyronnet, S., Imataka, H., Gingras, A., Fukunaga, R., Hunter, T., & Sonenberg, N. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.270 · Cited by 639
Signaling Pathways and Molecular Mechanisms through which Branched-Chain Amino Acids Mediate Translational Control of Protein Synthesis
Kimball, S. R., & Jefferson, L. S. (2006) · Journal of Nutrition · doi:10.1093/jn/136.1.227s · Cited by 637
Disruption of the p70s6k/p85s6k gene reveals a small mouse phenotype and a new functional S6 kinase
Shima, H., Pende, M., Chen, Y., Fumagalli, S., THOMAS, G. V., & Kozma, S. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6649 · Cited by 636
Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase‐1 and p70 S6 kinase
Alessi, D. R., Barry Caudwell, F., Andjelkovic, M., Hemmings, B. A., & Cohen, P. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01370-1 · Cited by 628
Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family.
Jefferies, H. B. J., Reinhard, C., Kozma, S. C., & Thomas, G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4441 · Cited by 623
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) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00257.x · Cited by 615
Hypoxia-induced energy stress regulates mRNA translation and cell growth
Liu, L., Cash, T. P., Jones, R. G., Keith, B., Thompson, C. B., & Simon, M. C. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.010 · Cited by 607
mTOR, translation initiation and cancer
Mamane, Y., Petroulakis, E., LeBacquer, O., & Sonenberg, N. (2006) · Oncogene · doi:10.1038/sj.onc.1209888 · Cited by 607
The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
Ruggero, D., Montanaro, L., Ma, L., Xu, W. G., Londei, P., Cordon‐Cardo, C., & Pandolfi, P. P. (2004) · Nature Medicine · doi:10.1038/nm1042 · Cited by 592
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., Gradi, A., & Sonenberg, N. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7480 · Cited by 572
Ribosome biogenesis and cell growth: mTOR coordinates transcription by all three classes of nuclear RNA polymerases
Mayer, C., & Grummt, I. (2006) · Oncogene · doi:10.1038/sj.onc.1209883 · Cited by 568
The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity
Shahbazian, D., Roux, P. P., Mieulet, V., Cohen, M. S., Raught, B., Taunton, J., Hershey, J. W. B., Blenis, J., Pende, M., & Sonenberg, N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601166 · Cited by 532
TOS Motif-Mediated Raptor Binding Regulates 4E-BP1 Multisite Phosphorylation and Function
Schalm, S. S., Fingar, D. C., Sabatini, D. M., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00329-4 · Cited by 528
An expanding role for mTOR in cancer
Guertin, D. A., & Sabatini, D. M. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.06.007 · Cited by 522
Mnk2 and Mnk1 Are Essential for Constitutive and Inducible Phosphorylation of Eukaryotic Initiation Factor 4E but Not for Cell Growth or Development
Ueda, T., Watanabe-Fukunaga, R., Fukuyama, H., Nagata, S., & Fukunaga, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.15.6539-6549.2004 · Cited by 507
Identification of a Conserved Motif Required for mTOR Signaling
Schalm, S. S., & Blenis, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00762-5 · Cited by 490
Rheb fills a GAP between TSC and TOR
Manning, B. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.003 · Cited by 483
Endotoxin-responsive sequences control cachectin/tumor necrosis factor biosynthesis at the translational level.
Han, J. S., Brown, T., & Beutler, B. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.171.2.465 · Cited by 477
Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases
Raught, B., Peiretti, F., Gingras, A., Livingstone, M., Shahbazian, D., Mayeur, G. L., Polakiewicz, R. D., Sonenberg, N., & Hershey, J. W. B. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600193 · Cited by 473
mTOR and cancer therapy
Easton, J. B., & Houghton, P. J. (2006) · Oncogene · doi:10.1038/sj.onc.1209886 · Cited by 468
Activation of AMP-Activated Protein Kinase Leads to the Phosphorylation of Elongation Factor 2 and an Inhibition of Protein Synthesis
Horman, S., Browne, G. J., Krause, U., Patel, J. V., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C. G., & Rider, M. H. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01077-1 · Cited by 467
Rapamycin Attenuates Load-Induced Cardiac Hypertrophy in Mice
Shioi, T., McMullen, J. R., Tarnavski, O., Converso, K. L., Sherwood, M. C., Manning, W. J., & Izumo, S. (2003) · Circulation · doi:10.1161/01.cir.0000057979.36322.88 · Cited by 465
PI 3-kinase related kinases: ?big? players in stress-induced signaling pathways
Abraham, R. T. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.04.002 · Cited by 461
Hypoinsulinaemia, glucose intolerance and diminished β-cell size in S6K1-deficient mice
Pende, M., Kozma, S. C., Jaquet, M., Oorschot, V. M. J., Burcelin, R., MARCHAND‐BRUSTEL, Y. L., Klumperman, J., Thorens, B., & Thomas, G. W. (2000) · Nature · doi:10.1038/35050135 · Cited by 452
Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter
Leegwater, P., Vermeulen, G., Könst, A. A. M., Naidu, S., Mulders, J., Visser, A., Kersbergen, P., Mobach, D., Fonds, D., van Berkel, C. V., et al. (2001) · Nature Genetics · doi:10.1038/ng764 · Cited by 414
Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E.
Rousseau, D. L., Kaspar, R. L., Rosenwald, I. B., Gehrke, L., & Sonenberg, N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1065 · Cited by 401
Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
Welsh, G. I., & Proud, C. G. (1993) · Biochemical Journal · doi:10.1042/bj2940625 · Cited by 397
Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?
Corradetti, M. N., & Guan, K.-L. (2006) · Oncogene · doi:10.1038/sj.onc.1209885 · Cited by 396
MK2 Targets AU-rich Elements and Regulates Biosynthesis of Tumor Necrosis Factor and Interleukin-6 Independently at Different Post-transcriptional Levels
Neininger, A., Kontoyiannis, D. L., Kotlyarov, A., Winzen, R., Eckert, R., Volk, H., Holtmann, H., Kollias, G. A., & Gaestel, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100685200 · Cited by 394
Adipose tissue reduction in mice lacking the translational inhibitor 4E-BP1
Tsukiyama–Kohara, K., Poulin, F., Kohara, M., DeMaria, C. T., Cheng, A., Wu, Z., Gingras, A., Katsume, A., Elchebly, M., Spiegelman, B. M., et al. (2001) · Nature Medicine · doi:10.1038/nm1001-1128 · Cited by 392
Mitogen-Activated Protein Kinase-Activated Protein Kinase 2 Regulates Tumor Necrosis Factor mRNA Stability and Translation Mainly by Altering Tristetraprolin Expression, Stability, and Binding to Adenine/Uridine-Rich Element
Hitti, E., Iakovleva, T., Brook, M., Deppenmeier, S., Gruber, A. D., Radzioch, D., Clark, A. R., Blackshear, P. J., Kotlyarov, A., & Gaestel, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2399-2407.2006 · Cited by 389
NMDA receptor-mediated control of protein synthesis at developing synapses
Scheetz, A., Nairn, A., & Constantine-Paton, M. (2000) · Nature Neuroscience · doi:10.1038/72915 · Cited by 382
The role of c-myc in cellular growth control
Schmidt, E. V. (1999) · Oncogene · doi:10.1038/sj.onc.1202751 · Cited by 380
Regulation of the p70 S6 Kinase by Phosphorylation in Vivo
Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., Zhang, A., Comb, M. J., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16621 · Cited by 375
Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control
Koritzinsky, M., Magagnin, M. G., van den Beucken, T., Seigneuric, R., Savelkouls, K. G. M., Dostie, J., Pyronnet, S., Kaufman, R. J., Weppler, S. A., Voncken, J. W., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600998 · Cited by 369
AMP-Activated Protein Kinase Protects Cardiomyocytes against Hypoxic Injury through Attenuation of Endoplasmic Reticulum Stress
Terai, K., Hiramoto, Y., Masaki, M., Sugiyama, S., Kuroda, T., Hori, M., Kawase, I., & Hirota, H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9554-9575.2005 · Cited by 356
The Tuberous Sclerosis Protein TSC2 Is Not Required for the Regulation of the Mammalian Target of Rapamycin by Amino Acids and Certain Cellular Stresses
Smith, E. M., FINN, S. G., Tee, A. R., Browne, G. J., & Proud, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414499200 · Cited by 354
Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398
Browne, G. J., Finn, S. G., & Proud, C. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309773200 · Cited by 353
Rheb Binding to Mammalian Target of Rapamycin (mTOR) Is Regulated by Amino Acid Sufficiency
Long, X., Ortiz-Vega, S., Lin, Y., & Avruch, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500169200 · Cited by 349
Elevated sensitivity to diet-induced obesity and insulin resistance in mice lacking 4E-BP1 and 4E-BP2
Bacquer, O. L., Petroulakis, E., Paglialunga, S., Poulin, F., Richard, D., Cianflone, K., & Sonenberg, N. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29528 · Cited by 348
The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase
Woods, Y. L., Cohen, P., Becker, W. B., Jakes, R., Goedert, M., Wang, X., & Proud, C. G. (2001) · Biochemical Journal · doi:10.1042/bj3550609 · Cited by 343
Tuberous sclerosis: a GAP at the crossroads of multiple signaling pathways
Kwiatkowski, D. J., & Manning, B. D. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi260 · Cited by 332
hnRNP A1 Relocalization to the Stress Granules Reflects a Role in the Stress Response
Guil, S., Long, J. C., & Cáceres, J. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00224-06 · Cited by 318
The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation
Dean, J. L. E., Sully, G., Clark, A. R., & Saklatvala, J. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.04.006 · Cited by 312
Does phosphorylation of the cap‐binding protein eIF4E play a role in translation initiation?
Scheper, G. C., & Proud, C. G. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03291.x · Cited by 310
Serum‐stimulated, rapamycin‐sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
Raught, B., Gingras, A., Gygi, S. P., Imataka, H., Morino, S., Gradi, A., Aebersold, R., & Sonenberg, N. (2000) · EMBO Journal · doi:10.1093/emboj/19.3.434 · Cited by 306
Amino Acid-Induced Translation of TOP mRNAs Is Fully Dependent on Phosphatidylinositol 3-Kinase-Mediated Signaling, Is Partially Inhibited by Rapamycin, and Is Independent of S6K1 and rpS6 Phosphorylation
Tang, H., Hornstein, E., Stolovich, M., Levy, G., Livingstone, M., Templeton, D. J., Avruch, J., & Meyuhas, O. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8671-8683.2001 · Cited by 304
Insulin and amino-acid regulation of mTOR signaling and kinase activity through the Rheb GTPase
Avruch, J., Hara, K., Lin, Y., Liu, M., Long, X., Ortiz-Vega, S., & Yonezawa, K. (2006) · Oncogene · doi:10.1038/sj.onc.1209882 · Cited by 301
Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase‐3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
Welsh, G. I., Miller, C. M., Loughlin, A. J., & Price, N. T. (1998) · FEBS Letters · doi:10.1016/s0014-5793(97)01548-2 · Cited by 298
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., Flynn, A., Waskiewicz, A. J., Webb, B. L. J., Vries, R. G. J., Baines, I. A., Cooper, J. A., & Proud, C. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9373 · Cited by 296
The Translation Repressor 4E-BP2 Is Critical for eIF4F Complex Formation, Synaptic Plasticity, and Memory in the Hippocampus
Banko, J. L., Poulin, F., Hou, L., DeMaria, C. T., Sonenberg, N., & Klann, E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2423-05.2005 · Cited by 290
Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E
Rosenwald, I. B., Lazaris-Karatzas, A., Sonenberg, N., & Schmidt, E. V. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7358 · Cited by 287
Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form.
Minich, W. B., Balasta, M. L., Goss, D. J., & Rhoads, R. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7668 · Cited by 286
Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity
Yamaguchi, H. Q., Matsushita, M., Nairn, A. C., & Kuriyan, J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00256-8 · Cited by 279
Functional properties of phosphorylated elongation factor 2
CARLBERG, U., NILSSON, A., & Nygârd, O. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19169.x · Cited by 278
MAPKAP Kinase 2 Phosphorylates Tristetraprolin on in Vivo Sites Including Ser178, a Site Required for 14-3-3 Binding
Chrestensen, C. A., Schroeder, M. J., Shabanowitz, J., Hunt, D. F., Pelo, J. W., Worthington, M., & Sturgill, T. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310486200 · Cited by 273
Regulation of translation elongation factor‐2 by insulin via a rapamycin‐sensitive signalling pathway.
Redpath, N. T., Foulstone, E. J., & Proud, C. G. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00582.x · Cited by 265
Phosphorylation of Eukaryotic Initiation Factor 4E Markedly Reduces Its Affinity for Capped mRNA
Scheper, G. C., van Kollenburg, B., Hu, J., Luo, Y., Goss, D. J., & Proud, C. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m103607200 · Cited by 257
A Novel mTOR-Regulated Phosphorylation Site in Elongation Factor 2 Kinase Modulates the Activity of the Kinase and Its Binding to Calmodulin
Browne, G. J., & Proud, C. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2986-2997.2004 · Cited by 256
A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38δ
Knebel, A., Morrice, N., & Cohen, P. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4360 · Cited by 254
The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores
Maurin, A., Jousse, C., Avérous, J., Parry, L., Bruhat, A., Chérasse, Y., Zeng, H., Zhang, Y., Harding, H. P., Ron, D., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.03.004 · Cited by 240
The Stress-inducted Proteins RTP801 and RTP801L Are Negative Regulators of the Mammalian Target of Rapamycin Pathway
Corradetti, M. N., Inoki, K., & Guan, K.-L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c400557200 · Cited by 237
Hypoxia Inhibits Protein Synthesis through a 4E-BP1 and Elongation Factor 2 Kinase Pathway Controlled by mTOR and Uncoupled in Breast Cancer Cells
Connolly, E. P., Braunstein, S. E., Formenti, S. C., & Schneider, R. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3955-3965.2006 · Cited by 227
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. (2003) · Clinical & Experimental Metastasis · doi:10.1023/a:1022943419011 · Cited by 219
Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP‐K2 and its interaction with cytokine mRNAs
Rousseau, S., Morrice, N., Peggie, M., Campbell, D. G., Gaestel, M., & Cohen, P. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf639 · Cited by 219
The Mitogen-Activated Protein Kinase (MAPK)-Activated Protein Kinases MK2 and MK3 Cooperate in Stimulation of Tumor Necrosis Factor Biosynthesis and Stabilization of p38 MAPK
Ronkina, N., Kotlyarov, A., Dittrich‐Breiholz, O., Kracht, M., Hitti, E., Milarski, K. L., Askew, R., Marušić, S., Lin, L.-L., Gaestel, M., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01456-06 · Cited by 217
Phosphorylation of Eukaryotic Protein Synthesis Initiation Factor 4E at Ser-209
Joshi, B., Cai, A., Keiper, B. D., Minich, W. B., Méndez, R., Beach, C. M., Stȩpiński, J., Stolarski, R., Darżynkiewicz, E., & Rhoads, R. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14597 · Cited by 216
The Mnks Are Novel Components in the Control of TNFα Biosynthesis and Phosphorylate and Regulate hnRNP A1
Buxadé, M., Parra-Palau, J. L., Rousseau, S., Shpiro, N., Márquez, R., MORRICE, N. A., Bain, J., Espel, E., & Proud, C. G. (2005) · Immunity · doi:10.1016/j.immuni.2005.06.009 · Cited by 215
Quantitative phosphorylation profiling of the ERK/p90 ribosomal S6 kinase-signaling cassette and its targets, the tuberous sclerosis tumor suppressors
Ballif, B. A., Roux, P. P., Gerber, S. A., MacKeigan, J. P., Blenis, J., & Gygi, S. P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409143102 · Cited by 211
United at last: the tuberous sclerosis complex gene products connect the phosphoinositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signalling
Manning, B. D., & Cantley, L. C. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310573 · Cited by 211
Differences in the way a mammalian cell and yeast cells coordinate cell growth and cell-cycle progression
Conlon, I. J., & RAFF, M. C. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-7 · Cited by 208
Distinct Signaling Events Downstream of mTOR Cooperate To Mediate the Effects of Amino Acids and Insulin on Initiation Factor 4E-Binding Proteins
Wang, X., Beugnet, A., Murakami, M., Yamanaka, S., & Proud, C. G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2558-2572.2005 · Cited by 207
eIF4E promotes nuclear export of cyclin D1 mRNAs via an element in the 3′UTR
Čuljković, B., Topisirović, I., Skrabanek, L. A., Ruiz‐Gutierrez, M., & Borden, K. L. B. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200501019 · Cited by 207
The Mitogen-Activated Protein Kinase Signal-Integrating Kinase Mnk2 Is a Eukaryotic Initiation Factor 4E Kinase with High Levels of Basal Activity in Mammalian Cells
Scheper, G. C., MORRICE, N. A., Kleijn, M., & Proud, C. G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.743-754.2001 · Cited by 202
When translation meets transformation: the mTOR story
Avérous, J., & Proud, C. G. (2006) · Oncogene · doi:10.1038/sj.onc.1209887 · Cited by 197
Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cellsPreprint
Walsh, D., & Mohr, I. (2004) · Genes & Development · doi:10.1101/gad.1185304 · Cited by 192
Identification of Phosphorylation Sites in the Translational Regulator, PHAS-I, That Are Controlled by Insulin and Rapamycin in Rat Adipocytes
Fadden, P., Haystead, T., & Lawrence, J. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.10240 · Cited by 191
The p70 S6 Kinase Integrates Nutrient and Growth Signals to Control Translational Capacity
Avruch, J., BELHAM, C. M., Weng, Q. P., Hara, K., & Yonezawa, K. (2001) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-56688-2_5 · Cited by 181
Phosphorylation of Eukaryotic Translation Initiation Factor 4E Is Critical for Growth
Lachance, P. E. D., Miron, M., Raught, B., Sonenberg, N., & Lasko, P. F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.6.1656-1663.2002 · Cited by 180
Alpha-kinases: a new class of protein kinases with a novel catalytic domain
Ryazanov, A. G., Pavur, K. S., & Dorovkov, M. V. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80006-2 · Cited by 179
Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors
Patel, J. C., McLeod, L. E., Vries, R. G. J., Flynn, A., Wang, X., & Proud, C. G. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02992.x · Cited by 171
Rapamycin Inhibits α 1 -Adrenergic Receptor–Stimulated Cardiac Myocyte Hypertrophy but Not Activation of Hypertrophy-Associated Genes
Boluyt, M. O., Zheng, J.-S., Younès, A., Long, X., O’Neill, L., Silverman, H. S., Lakatta, E. G., & Crow, M. T. (1997) · Circulation Research · doi:10.1161/01.res.81.2.176 · Cited by 167
Role of Translation Initiation Factor 2B in Control of Cell Survival by the Phosphatidylinositol 3-Kinase/Akt/Glycogen Synthase Kinase 3β Signaling Pathway
Pap, M., & Cooper, G. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.2.578-586.2002 · Cited by 165
The p38 and MK2 Kinase Cascade Phosphorylates Tuberin, the Tuberous Sclerosis 2 Gene Product, and Enhances Its Interaction with 14-3-3
Li, Y., Inoki, K., Vacratsis, P. O., & Guan, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300862200 · Cited by 163
Regulation of heterogenous nuclear ribonucleoprotein A1 transport by phosphorylation in cells stressed by osmotic shock
Allemand, E., Guil, S., Myers, M. P., Moscat, J., Cáceres, J. F., & Krainer, A. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409889102 · Cited by 161
Malignant transformation by overproduction of translation initiation factor eIF4G.
Shimogori, T., Ishii, I., Kashiwagi, K., Mashiba, H., EKIMOTO, H., & Igarashi, K. (1997) · PubMed · Cited by 159
Elongation factor‐2 kinase and its newly discovered relatives
Ryazanov, A. G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02299-8 · Cited by 152
Cardiac hypertrophy: A matter of translation
Hannan, R. D., Jenkins, A., Jenkins, A., & Brandenburger, Y. (2003) · Clinical and Experimental Pharmacology and Physiology · doi:10.1046/j.1440-1681.2003.03873.x · Cited by 150
MAPKAP Kinase 2-Deficient Mice Are Resistant to Collagen-Induced Arthritis
Hegen, M., Gaestel, M., Nickerson‐Nutter, C. L., Lin, L., & Telliez, J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.3.1913 · Cited by 147
The 5' Terminal Oligopyrimidine Tract Confers Translational Control on Top Mrnas in a Cell Type-and Sequence Context-Dependent Manner
Avni, D., Biberman, Y., & Meyuhas, O. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.5.995 · Cited by 140
Caspase Cleavage of Initiation Factor 4E-Binding Protein 1 Yields a Dominant Inhibitor of Cap-Dependent Translation and Reveals a Novel Regulatory Motif
Tee, A. R., & Proud, C. G. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.6.1674-1683.2002 · Cited by 139
Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled repressor and by the double-stranded RNA-activated inhibitor
Colthurst, D. R., Campbell, D. G., & Proud, C. G. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13523.x · Cited by 134
mTOR‐dependent stimulation of the association of eIF4G and eIF3 by insulin
Harris, T. E., Chi, A., Shabanowitz, J., Hunt, D. F., Rhoads, R. E., & Lawrence, J. C. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601047 · Cited by 133
Deletion of Ribosomal S6 Kinases Does Not Attenuate Pathological, Physiological, or Insulin-Like Growth Factor 1 Receptor-Phosphoinositide 3-Kinase-Induced Cardiac Hypertrophy
McMullen, J., Shioi, T., Zhang, L., Tarnavski, O., Sherwood, M., Dorfman, A., Longnus, S., Pende, M., Martin, K., Blenis, J., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.14.6231-6240.2004 · Cited by 133
Mammalian Target of Rapamycin-dependent Phosphorylation of PHAS-I in Four (S/T)P Sites Detected by Phospho-specific Antibodies
Mothe‐Satney, I., Brunn, G. J., McMahon, L. P., Capaldo, C., Abraham, R. T., & Lawrence, J. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006005200 · Cited by 130
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. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00422-5 · Cited by 130
The emerging roles of translation factor eIF4E in the nucleus
Strudwick, S., & Borden, K. L. B. (2002) · Differentiation · doi:10.1046/j.1432-0436.2002.700102.x · Cited by 129
Mutations Linked to Leukoencephalopathy with Vanishing White Matter Impair the Function of the Eukaryotic Initiation Factor 2B Complex in Diverse Ways
Li, W., Wang, X.-M., van der Knaap, M. S., & Proud, C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3295-3306.2004 · Cited by 126
Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2)
Rolfe, M. J., McLeod, L. E., Pratt, P. F., & Proud, C. G. (2005) · Biochemical Journal · doi:10.1042/bj20041888 · Cited by 124
Eukaryotic initiation factor 2B: identification of multiple phosphorylation sites in the ϵ‐subunit and their functions in vivo
Wang, X., Paulin, F. E. M., Campbell, L. E., Gomez, E., O'Brien, K., Morrice, N., & Proud, C. G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4349 · Cited by 121
Myocardial Ischemia and Increased Heart Work Modulate the Phosphorylation State of Eukaryotic Elongation Factor-2
Horman, S., Beauloye, C., Vertommen, D., Vanoverschelde, J., Hue, L., & Rider, M. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302403200 · Cited by 121
Characterization of the minimal catalytic domain within eIF2B: the guanine‐nucleotide exchange factor for translation initiation
Gomez, E., Mohammad, S. S., & Pavitt, G. (2002) · EMBO Journal · doi:10.1093/emboj/cdf515 · Cited by 120
Elongation factor-1 alpha mRNA is selectively translated following mitogenic stimulation.
Jefferies, H. B. J., Thomas, G., & Thomas, G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41789-3 · Cited by 117
Biology of tumor cell invasion: Interplay of cell adhesion and matrix degradation
Heino, J. (1996) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19960315)65:6 · Cited by 117
The C Terminus of Initiation Factor 4E-Binding Protein 1 Contains Multiple Regulatory Features That Influence Its Function and Phosphorylation
Wang, X., Li, W., Parra, J.-L., Beugnet, A., & Proud, C. G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1546-1557.2003 · Cited by 116
The large spectrum of eIF2B-related diseases
Fogli, A., & Boespflug‐Tanguy, O. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340022 · Cited by 115
eEF1B: At the dawn of the 21st century
Sourd, F. L., Boulben, S., Bouffant, R. L., Cormier, P., Morales, J., Bellé, R., & Mulner‐Lorillon, O. (2006) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2006.02.003 · Cited by 114
Translation Factor eIF4E Rescues Cells from Myc-dependent Apoptosis by Inhibiting Cytochromec Release
Li, S., Takasu, T., Perlman, D., Peterson, M. S., Burrichter, D., Avdulov, S. V., Bitterman, P. B., & Polunovsky, V. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208821200 · Cited by 114
Mutations Causing Childhood Ataxia with Central Nervous System Hypomyelination Reduce Eukaryotic Initiation Factor 2B Complex Formation and Activity
Richardson, J. P., Mohammad, S. S., & Pavitt, G. D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2352-2363.2004 · Cited by 114
Adenovirus‐specific translation by displacement of kinase Mnk1 from cap‐initiation complex eIF4F
Cuesta, R., Xi, Q., & Schneider, R. J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3465 · Cited by 113
The Rapamycin-Binding Domain Governs Substrate Selectivity by the Mammalian Target of Rapamycin
McMahon, L. P., Choi, K. M., Lin, T.-A., Abraham, R. T., & Lawrence, J. C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7428-7438.2002 · Cited by 113
The life and death of translation elongation factor 2
Merrill, A. R., Jørgensen, R., & Andersen, G. R. (2005) · Biochemical Society Transactions · doi:10.1042/bst20060001 · Cited by 112
Identification of the phosphorylation sites in elongation factor‐2 from rabbit reticulocytes
Price, N. T., Redpath, N. T., Severinov, K., Campbell, D. G., Russell, J., & Proud, C. G. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80489-p · Cited by 111
The N and C Termini of the Splice Variants of the Human Mitogen-Activated Protein Kinase-Interacting Kinase Mnk2 Determine Activity and Localization
Scheper, G. C., Parra-Palau, J. L., Wilson, M., van Kollenburg, B., Vertegaal, A. C. O., Han, Z., & Proud, C. G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5692-5705.2003 · Cited by 109
Distinct Signalling Pathways Mediate Insulin and Phorbol Ester-stimulated Eukaryotic Initiation Factor 4F Assembly and Protein Synthesis in HEK 293 Cells
Herbert, T. P., Kilhams, G. R., Batty, I. H., & Proud, C. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.11249 · Cited by 107
Inhibition of Myc-dependent apoptosis by eukaryotic translation initiation factor 4E requires cyclin D1
Tan, A., Bitterman, P. B., Sonenberg, N., Peterson, M., & Polunovsky, V. A. (2000) · Oncogene · doi:10.1038/sj.onc.1203446 · Cited by 106
The life and death of translation elongation factor 2
Jørgensen, R., Merrill, A. R., & Andersen, G. R. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340001 · Cited by 105
22 Translational Control of TOP mRNAsPreprint
Meyuhas, O., & Hornstein, E. (2000) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969618.39.671 · Cited by 101
The large spectrum of eIF2B-related diseases
Boespflug‐Tanguy, O., & Fogli, A. (2005) · Biochemical Society Transactions · doi:10.1042/bst20060022 · Cited by 99
T-cell Activation Leads to Rapid Stimulation of Translation Initiation Factor eIF2B and Inactivation of Glycogen Synthase Kinase-3
Welsh, G. I., Miyamoto, S., Price, N. T., Safer, B., & Proud, C. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11410 · Cited by 99
Translational control of gene expression in a normal fibroblast. Characterization of a subclass of mRNAs with unusual kinetic properties
Walden, W. E., & Thach, R. E. (1986) · Biochemistry · doi:10.1021/bi00356a030 · Cited by 96
Mechanisms of translational regulation in Drosophila
Wilhelm, J. E., & Smibert, C. A. (2005) · Biology of the Cell · doi:10.1042/bc20040097 · Cited by 94
13 eIF2α Phosphorylation in Cellular Stress Responses and DiseasePreprint
Ron, D., & Harding, H. (2007) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969767.48.345 · Cited by 92
Phosphorylation of Eukaryotic Translation Initiation Factor 2Bε by Glycogen Synthase Kinase-3β Regulates β-Adrenergic Cardiac Myocyte Hypertrophy
Hardt, S. E., Tomita, H., Katus, H. A., & Sadoshima, J. (2004) · Circulation Research · doi:10.1161/01.res.0000124977.59827.80 · Cited by 88
Translational Control of Gene ExpressionPreprint
Cline, A. L., & Bock, R. M. (1966) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1966.031.01.042 · Cited by 88
Hamartin and tuberin: Working together for tumour suppression
Jóźwiak, J. (2005) · International Journal of Cancer · doi:10.1002/ijc.21542 · Cited by 87
Cyclic AMP-dependent protein kinase phosphorylates rabbit reticulocyte elongation factor-2 kinase and induces calcium-independent activity
Redpath, N. T., & Proud, C. G. (1993) · Biochemical Journal · doi:10.1042/bj2930031 · Cited by 87
Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E
Herbert, T. P., Fåhræus, R., Prescott, A. R., Lane, D. P., & Proud, C. G. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00567-4 · Cited by 85
Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and −insensitive pathways
Knebel, A., Haydon, C. E., MORRICE, N. A., & Cohen, P. (2002) · Biochemical Journal · doi:10.1042/bj20020916 · Cited by 80
Nutrients differentially regulate multiple translation factors and their control by insulin
Campbell, L., Wang, X., & Proud, C. G. (1999) · Biochemical Journal · doi:10.1042/bj3440433 · Cited by 78
Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity
Diggle, T. A., Subkhankulova, T., Lilley, K. S., SHIKOTRA, N., Willis, A. E., & Redpath, N. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530621 · Cited by 77
Enhancement of translation elongation in neurons by brain‐derived neurotrophic factor: Implications for mammalian target of rapamycin signaling
Inamura, N., Nawa, H., & Takei, N. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03466.x · Cited by 75
mTOR and cancer: reason for dancing at the crossroads?
THOMAS, G. V. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.12.003 · Cited by 72
Stopped-flow Kinetic Analysis of eIF4E and Phosphorylated eIF4E Binding to Cap Analogs and Capped Oligoribonucleotides
Slepenkov, S. V., Darżynkiewicz, E., & Rhoads, R. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601653200 · Cited by 71
The Expression of Poly(A)-binding Protein Gene Is Translationally Regulated in a Growth-dependent Fashion through a 5′-Terminal Oligopyrimidine Tract Motif
Hornstein, E., Git, A., Braunstein, I., Avni, D., & Meyuhas, O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1708 · Cited by 71
Regulation of protein synthesis in Swiss 3T3 fibroblasts. Rapid activation of the guanine-nucleotide-exchange factor by insulin and growth factors
Welsh, G. I., & Proud, C. G. (1992) · Biochemical Journal · doi:10.1042/bj2840019 · Cited by 71
N -methyl- d -aspartate receptor activation and visual activity induce elongation factor-2 phosphorylation in amphibian tecta: A role for N -methyl- d -aspartate receptors in controlling protein synthesis
Scheetz, A. J., Nairn, A. C., & Constantine‐Paton, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14770 · Cited by 70
Features of the Catalytic Domains and C Termini of the MAPK Signal-integrating Kinases Mnk1 and Mnk2 Determine Their Differing Activities and Regulatory Properties
Parra-Palau, J. L., Buxadé, M., & Proud, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508356200 · Cited by 69
Affinity purification of ARE-binding proteins identifies poly(A)-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization
Bollig, F., Winzen, R., Gaestel, M., Kostka, S., Resch, K., & Holtmann, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00015-9 · Cited by 69
3 The Protein Biosynthesis, Elongation Cycle
Merrick, W. C., & Nyborg, J. (2000) · doi:10.1101/087969618.39.89 · Cited by 69
Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1
O’Loghlen, A., González, V. M., Piñeiro, D., Pérez-Morgado, M. I., Salinas, M., & Martín, M. E. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.06.006 · Cited by 67
Two Different Signal Transduction Pathways Are Implicated in the Regulation of Initiation Factor 2B Activity in Insulin-like Growth Factor-1-stimulated Neuronal Cells
Quevedo, C., Alcázar, A., & Salinas, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000238200 · Cited by 67
Crystal Structures of the Mnk2 Kinase Domain Reveal an Inhibitory Conformation and a Zinc Binding Site
Jauch, R., Jäkel, S., Netter, C., Schreiter, K., Aicher, B., Jäckle, H., & Wahl, M. C. (2005) · Structure · doi:10.1016/j.str.2005.07.013 · Cited by 67
Regulation of matrix metalloproteinase-9 (MMP-9) by translational efficiency in murine prostate carcinoma cells.
Jiang, Y., & Muschel, R. J. (2002) · PubMed · Cited by 66
An activity-dependent switch to cap-independent translation triggered by eIF4E dephosphorylation
Dyer, J. R., Michel, S. H., Lee, W., Castellucci, V. F., Wayne, N. L., & Sossin, W. S. (2003) · Nature Neuroscience · doi:10.1038/nn1018 · Cited by 63
ATP depletion increases phosphorylation of elongation factor eEF2 in adult cardiomyocytes independently of inhibition of mTOR signalling
McLeod, L. E., & Proud, C. G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03582-2 · Cited by 61
Nerve and Epidermal Growth Factor Induce Protein Synthesis and eIF2B Activation in PC12 Cells
Kleijn, M., Welsh, G. I., Scheper, G. C., Voorma, H. O., Proud, C. G., & Thomas, A. A. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5536 · Cited by 60
Regulation of the phosphorylation of elongation factor 2 by MEK‐dependent signalling in adult rat cardiomyocytes
Wang, L., & Proud, C. G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03536-6 · Cited by 59
Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity
Diggle, T. A., Subkhankulova, T., Lilley, K. S., et al. (2001) · Biochemical Journal · doi:10.1042/bj3530621 · Cited by 56
Identification of the Human Mnk2 Gene (MKNK2) through Protein Interaction with Estrogen Receptor β
Slentz‐Kesler, K., Moore, J. T., Lombard, M., Zhang, J., Hollingsworth, R. E., & Weiner, M. P. (2000) · Genomics · doi:10.1006/geno.2000.6299 · Cited by 55
Regulation of protein-synthesis elongation-factor-2 kinase by cAMP in adipocytes
Diggle, T. A., Redpath, N. T., Heesom, K. J., & Denton, R. M. (1998) · Biochemical Journal · doi:10.1042/bj3360525 · Cited by 54

Flagged first, then by citations

9 of the 226 references couldn’t be matched to a known paper.

Research works printed but not linked: 5

Hinnebusch, 2000, Mechanism and regulation of methionyl-tRNA binding to ribosomes, 185
Pestova, 2006, The mechanism of translation initiation in eukaryotes, 87
Dever, 2006, The eIF2α kinases, 319
Klann, 2006, Protein synthesis and translational control in synaptic plasticity and learning and memory, 485
Shantz, 1994, Regulation of ornithine decarboxylase (ODC) expression by translation initiation factor eIF-4E, FASEB J., 8, A1309

Sorted by citations

Mechanisms of Cancer Cachexia
Tisdale, M. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00016.2008 · Cited by 1,216
Profiling translatomes of discrete cell populations resolves altered cellular priorities during hypoxia in Arabidopsis
Mustroph, A., Zanetti, M. E., Jang, C. J. H., Holtan, H., Repetti, P. P., Galbraith, D. W., Girke, T., & Bailey-Serres, J. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906131106 · Cited by 644
Regulation of macroautophagy by mTOR and Beclin 1 complexes
Pattingre, S., Espert, L., Biard‐Piechaczyk, M., & Codogno, P. (2007) · Biochimie · doi:10.1016/j.biochi.2007.08.014 · Cited by 535
The Arc of synaptic memory
Bramham, C. R., Alme, M. N., Bittins, M., Kuipers, S. D., Nair, R. R., Pai, B., Panja, D., Schubert, M., Soule, J., Tiron, A., et al. (2010) · Experimental Brain Research · doi:10.1007/s00221-009-1959-2 · Cited by 452
mTOR and autophagy: A dynamic relationship governed by nutrients and energy
Dunlop, E. A., & Tee, A. R. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.08.006 · Cited by 452

See all 520

Authors: Proud, C. G.
Affiliations: University of British Columbia (CA)
Corresponding author: Proud, Christopher G.
ORCID: Proud, Christopher G.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2007-03-26
Volume: 403
Issue: 2
Pages: 217-234
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20070024
OpenAlex: W2080451230
Cited by: 520
References: 226
Citations by year: 2026: 5 · 2025: 6 · 2024: 8 · 2023: 10 · 2022: 10 · 2021: 11 · 2020: 14 · 2019: 17 · 2018: 21 · 2017: 20 · 2016: 21 · 2015: 26 · 2014: 29 · 2013: 37 · 2012: 50
FWCI: 4.88
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (submittedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Keywords: translational regulation, signal transduction, protein synthesis, mTOR, mitogen-activated protein kinase, RNA-binding proteins, mRNA stability, cell growth, nutrient signaling, energy status, hormone signaling, growth factor signaling, cancer, neurodegeneration, tissue hypertrophy
MeSH terms: Animals, Humans, Protein Binding, Ribosomes, Protein Biosynthesis, Signal Transduction, RNA-Binding Proteins

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Signalling to translation: how signal transduction pathways control the protein synthetic machinery

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