Translational control of immune responses: From transcripts to translatomes

Nature Immunology

Volumn 15, Issue 6, 2014, Pages 503-511

  Piccirillo, Ciriaco A ^a,b   Bjur, Eva ^c   Topisirovic, Ivan ^a,d   Sonenberg, Nahum ^e   Larsson, Ola ^c  

^a MCGILL UNIVERSITY   (Canada)

^b RESEARCH INSTITUTE OF THE MCGILL UNIVERSITY HEALTH CENTRE   (Canada)

^c KAROLINSKA INSTITUTE   (Sweden)

^d MCGILL UNIVERSITY   (Canada)

^e MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4E; INITIATION FACTOR 4E BINDING PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1;

GENE EXPRESSION; GENE EXPRESSION REGULATION; GENETIC ASSOCIATION; HUMAN; IMMUNE RESPONSE; IMMUNE SYSTEM; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; REVIEW; RIBOSOME; RNA TRANSLATION; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; EUKARYOTIC INITIATION FACTOR-4E; GENE EXPRESSION REGULATION; HUMANS; IMMUNE SYSTEM; MICE; MULTIPROTEIN COMPLEXES; PHOSPHOPROTEINS; PROTEIN BIOSYNTHESIS; RNA, MESSENGER; TOR SERINE-THREONINE KINASES; TRANSCRIPTION, GENETIC;

EID: 84901057834     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.2891     Document Type: Review

References (132)

1. Bava, F.A. et al. CPEB1 coordinates alternative 3′-UTR formation with translational regulation. Nature 495, 121-125 (2013
2. Rousseau, D., Kaspar, R., Rosenwald, I., Gehrke, L. & Sonenberg, N. Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E. Proc. Natl. Acad. Sci. USA 93, 1065-1070 (1996
3. Lindstein, T., June, C.H., Ledbetter, J.A., Stella, G. & Thompson, C.B. Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway. Science 244, 339-343 (1989
4. Schena, M. et al. Parallel human genome analysis: Microarray-based expression monitoring of 1000 genes. Proc. Natl. Acad. Sci. USA 93, 10614-10619 (1996
5. Schena, M., Shalon, D., Davis, R.W. & Brown, P.O. Quantitative monitoring of gene expression patterns with a complementary DNA microarray. Science 270, 467-470 (1995
6. Lockhart, D.J. et al. Expression monitoring by hybridization to high-density oligonucleotide arrays. Nat. Biotechnol. 14, 1675-1680 (1996
7. Larsson, O., Tian, B. & Sonenberg, N. Toward a genome-wide landscape of translational control. Cold Spring Harb. Perspect. Biol. 5, a012302 (2013
8. Vogel, C. & Marcotte, E.M. Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat. Rev. Genet. 13, 227-232 (2012
9. Schwanhäusser, B. et al. Global quantification of mammalian gene expression control. Nature 473, 337-342 (2011
10. Kristensen, A.R., Gsponer, J. & Foster, L.J. Protein synthesis rate is the predominant regulator of protein expression during differentiation. Mol. Syst. Biol. doi:10.1038/msb.2013.47 (17 September 2013
11. Spirin, A.S. The second Sir Hans Krebs lecture. Informosomes. Eur. J. Biochem. 10, 20-35 (1969
12. Keene, J.D. & Tenenbaum, S.A. Eukaryotic mRNPs may represent posttranscriptional operons. Mol. Cell 9, 1161-1167 (2002
13. Candeias, M.M. et al. P53 mRNA controls p53 activity by managing Mdm2 functions. Nat. Cell Biol. 10, 1098-1105 (2008
14. Hershey, J.W., Sonenberg, N. & Mathews, M.B. Principles of translational control: An overview. Cold Spring Harb. Perspect. Biol. 4, a011528 (2012
15. Shalgi, R. et al. Widespread regulation of translation by elongation pausing in heat shock. Mol. Cell 49, 439-452 (2013
16. Liu, B., Han, Y. & Qian, S.B. Cotranslational response to proteotoxic stress by elongation pausing of ribosomes. Mol. Cell 49, 453-463 (2013
17. Gerashchenko, M.V., Lobanov, A.V. & Gladyshev, V.N. Genome-wide ribosome profiling reveals complex translational regulation in response to oxidative stress. Proc. Natl. Acad. Sci. USA 109, 17394-17399 (2012
18. Leprivier, G. et al. The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation. Cell 153, 1064-1079 (2013
19. Sonenberg, N. & Hinnebusch, A.G. Regulation of translation initiation in eukaryotes: Mechanisms and biological targets. Cell 136, 731-745 (2009
20. Jackson, R.J., Hellen, C.U. & Pestova, T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11, 113-127 (2010
21. Baltz, A.G. et al. The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46, 674-690 (2012
22. Castello, A. et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149, 1393-1406 (2012
23. Sabatini, D.M., Erdjument-Bromage, H., Lui, M., Tempst, P. & Snyder, S.H. RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78, 35-43 (1994
24. Brown, E.J. et al. A mammalian protein targeted by G1-Arresting rapamycin-receptor complex. Nature 369, 756-758 (1994
25. Gwinn, D.M. et al. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol. Cell 30, 214-226 (2008
26. Inoki, K., Zhu, T. & Guan, K.L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590 (2003
27. Corradetti, M.N., Inoki, K., Bardeesy, N., DePinho, R.A. & Guan, K.L. Regulation of the TSC pathway by LKB1: Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev. 18, 1533-1538 (2004
28. Shaw, R.J. et al. The LKB1 tumor suppressor negatively regulates mTOR signaling. Cancer Cell 6, 91-99 (2004
29. Hara, K. et al. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J. Biol. Chem. 273, 14484-14494 (1998
30. Wang, X., Campbell, L.E., Miller, C.M. & Proud, C.G. Amino acid availability regulates p70 S6 kinase and multiple translation factors. Biochem. J. 334, 261-267 (1998
31. DeYoung, M.P., Horak, P., Sofer, A., Sgroi, D. & Ellisen, L.W. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev. 22, 239-251 (2008
32. Brugarolas, J. et al. Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. Genes Dev. 18, 2893-2904 (2004
33. Laplante, M. & Sabatini, D.M. mTOR signaling in growth control and disease. Cell 149, 274-293 (2012
34. Kim, D.H. et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-175 (2002
35. Hara, K. et al. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 110, 177-189 (2002
36. Jacinto, E. et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6, 1122-1128 (2004
37. Sarbassov, D.D. et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14, 1296-1302 (2004
38. Sarbassov, D.D. et al. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol. Cell 22, 159-168 (2006
39. Heitman, J., Movva, N.R. & Hall, M.N. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 253, 905-909 (1991
40. Gingras, A.C. et al. Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism. Genes Dev. 13, 1422-1437 (1999
41. Brunn, G.J. et al. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J. 15, 5256-5267 (1996
42. Burnett, P.E., Barrow, R.K., Cohen, N.A., Snyder, S.H. & Sabatini, D.M. RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1. Proc. Natl. Acad. Sci. USA 95, 1432-1437 (1998
43. Hara, K. et al. Regulation of eIF-4E BP1 phosphorylation by mTOR. J. Biol. Chem. 272, 26457-26463 (1997
44. Wullschleger, S., Loewith, R. & Hall, M.N. TOR signaling in growth and metabolism. Cell 124, 471-484 (2006
45. Dorrello, N.V. et al. S6K1-And betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth. Science 314, 467-471 (2006
46. Raught, B. et al. Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases. EMBO J. 23, 1761-1769 (2004
47. Pause, A. et al. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371, 762-767 (1994
48. Roux, P.P. & Topisirovic, I. Regulation of mRNA translation by signaling pathways. Cold Spring Harb. Perspect. Biol. 4, a012252 (2012
49. Gingras, A.C. et al. Hierarchical phosphorylation of the translation inhibitor 4E-BP1. Genes Dev. 15, 2852-2864 (2001
50. Zimmer, S.G., DeBenedetti, A. & Graff, J.R. Translational control of malignancy: The mRNA cap-binding protein, eIF-4E, as a central regulator of tumor formation, growth, invasion and metastasis. Anticancer Res. 20, 3A, 1343-1351 (2000
51. Colina, R. et al. Translational control of the innate immune response through IRF-7. Nature 452, 323-328 (2008
52. Larsson, O. et al. Apoptosis resistance downstream of eIF4E: Posttranscriptional activation of an anti-Apoptotic transcript carrying a consensus hairpin structure. Nucleic Acids Res. 34, 4375-4386 (2006
53. Hsieh, A.C. et al. The translational landscape of mTOR signalling steers cancer initiation and metastasis. Nature 485, 55-61 (2012
54. Thoreen, C.C. et al. A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 485, 109-113 (2012
55. Bilanges, B. et al. Tuberous sclerosis complex proteins 1 and 2 control serum-dependent translation in a TOP-dependent and-independent manner. Mol. Cell. Biol. 27, 5746-5764 (2007
56. Patursky-Polischuk, I. et al. The TSC-mTOR pathway mediates translational activation of TOP mRNAs by insulin largely in a raptor-or rictor-independent manner. Mol. Cell. Biol. 29, 640-649 (2009
57. Avni, D., Shama, S., Loreni, F. & Meyuhas, O. Vertebrate mRNAs with a 5′-Terminal pyrimidine tract are candidates for translational repression in quiescent cells: Characterization of the translational cis-regulatory element. Mol. Cell. Biol. 14, 3822-3833 (1994
58. Miloslavski, R. et al. Oxygen sufficiency controls TOP mRNA translation via the TSC-Rheb-mTOR pathway in a 4E-BP-independent manner. J. Mol. Cell Biol. doi:10.1093/jmcb/mju008 (13 March 2014
59. Shama, S., Avni, D., Frederickson, R.M., Sonenberg, N. & Meyuhas, O. Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells. Gene Expr. 4, 241-252 (1995
60. Damgaard, C.K. & Lykke-Andersen, J. Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR. Genes Dev. 25, 2057-2068 (2011
61. Tcherkezian, J. et al. Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5′TOP mRNA translation. Genes Dev. 28, 357-371 (2014
62. Flynn, A. & Proud, C.G. Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-Treated Chinese hamster ovary cells. J. Biol. Chem. 270, 21684-21688 (1995
63. Fukunaga, R. & Hunter, T. MNK1, a new MAP kinase-Activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 16, 1921-1933 (1997
64. Waskiewicz, A.J., Flynn, A., Proud, C.G. & Cooper, J.A. Mitogen-Activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16, 1909-1920 (1997
65. Furic, L. et al. eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression. Proc. Natl. Acad. Sci. USA 107, 14134-14139 (2010
66. Fernandez, P.C. et al. Genomic targets of the human c-Myc protein. Genes Dev. 17, 1115-1129 (2003
67. Topisirovic, I. et al. Stability of eukaryotic translation initiation factor 4E mRNA is regulated by HuR, and this activity is dysregulated in cancer. Mol. Cell. Biol. 29, 1152-1162 (2009
68. Cook, K.D. & Miller, J. TCR-dependent translational control of GATA-3 enhances Th2 differentiation. J. Immunol. 185, 3209-3216 (2010
69. Gigoux, M. et al. Inducible costimulator facilitates T-dependent B cell activation by augmenting IL-4 translation. Mol. Immunol. 59, 46-54 (2014
70. Lee, M.S., Kim, B., Oh, G.T. & Kim, Y.J. OASL1 inhibits translation of the type I interferon-regulating transcription factor IRF7. Nat. Immunol. 14, 346-355 (2013
71. Bjur, E. et al. Distinct translational control in CD4+ T cell subsets. PLoS Genet. 9, e1003494 (2013
72. Tangye, S.G., Ma, C.S., Brink, R. & Deenick, E.K. The good, the bad and the ugly-TFH cells in human health and disease. Nat. Rev. Immunol. 13, 412-426 (2013
73. Araki, K., Ellebedy, A.H. & Ahmed, R. TOR in the immune system. Curr. Opin. Cell Biol. 23, 707-715 (2011
74. Xu, H. et al. Notch-RBP-J signaling regulates the transcription factor IRF8 to promote inflammatory macrophage polarization. Nat. Immunol. 13, 642-650 (2012
75. Herdy, B. et al. Translational control of the activation of transcription factor NF-κB and production of type I interferon by phosphorylation of the translation factor eIF4E. Nat. Immunol. 13, 543-550 (2012
76. Nikolcheva, T. et al. A translational rheostat for RFLAT-1 regulates RANTES expression in T lymphocytes. J. Clin. Invest. 110, 119-126 (2002
77. Krausgruber, T. et al. IRF5 promotes inflammatory macrophage polarization and TH1-TH17 responses. Nat. Immunol. 12, 231-238 (2011
78. Satoh, T. et al. The Jmjd3-Irf4 axis regulates M2 macrophage polarization and host responses against helminth infection. Nat. Immunol. 11, 936-944 (2010
79. Huang, J.T. & Schneider, R.J. Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein. Cell 65, 271-280 (1991
80. Kleijn, M., Vrins, C.L., Voorma, H.O. & Thomas, A.A. Phosphorylation state of the cap-binding protein eIF4E during viral infection. Virology 217, 486-494 (1996
81. Connor, J.H. & Lyles, D.S. Vesicular stomatitis virus infection alters the eIF4F translation initiation complex and causes dephosphorylation of the eIF4E binding protein 4E-BP1. J. Virol. 76, 10177-10187 (2002
82. Walsh, D. et al. Eukaryotic translation initiation factor 4F architectural alterations accompany translation initiation factor redistribution in poxvirus-infected cells. Mol. Cell. Biol. 28, 2648-2658 (2008
83. Walsh, D., Perez, C., Notary, J. & Mohr, I. Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J. Virol. 79, 8057-8064 (2005
84. Walsh, D. & Mohr, I. Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells. Genes Dev. 18, 660-672 (2004
85. Ben-Neriah, Y. & Karin, M. Inflammation meets cancer, with NF-κB as the matchmaker. Nat. Immunol. 12, 715-723 (2011
86. Vashchenko, G. & MacGillivray, R.T. Multi-copper oxidases and human iron metabolism. Nutrients 5, 2289-2313 (2013
87. Klebanoff, S.J. Bactericidal effect of Fe2+, ceruloplasmin, and phosphate. Arch. Biochem. Biophys. 295, 302-308 (1992
88. Mazumder, B. & Fox, P.L. Delayed translational silencing of ceruloplasmin transcript in γ interferon-Activated U937 monocytic cells: Role of the 3′ untranslated region. Mol. Cell. Biol. 19, 6898-6905 (1999
89. Sampath, P., Mazumder, B., Seshadri, V. & Fox, P.L. Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3′ untranslated region. Mol. Cell. Biol. 23, 1509-1519 (2003
90. Vyas, K. et al. Genome-wide polysome profiling reveals an inflammation-responsive posttranscriptional operon in gamma interferon-Activated monocytes. Mol. Cell. Biol. 29, 458-470 (2009
91. Mukhopadhyay, R. et al. DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression. Mol. Cell 32, 371-382 (2008
92. Scheu, S. et al. Activation of the integrated stress response during T helper cell differentiation. Nat. Immunol. 7, 644-651 (2006
93. Wek, R.C., Jiang, H.Y. & Anthony, T.G. Coping with stress: EIF2 kinases and translational control. Biochem. Soc. Trans. 34, 7-11 (2006
94. Villarino, A.V. et al. Posttranscriptional silencing of effector cytokine mRNA underlies the anergic phenotype of self-reactive T cells. Immunity 34, 50-60 (2011
95. Piecyk, M. et al. TIA-1 is a translational silencer that selectively regulates the expression of TNF-α. EMBO J. 19, 4154-4163 (2000
96. Katsanou, V. et al. HuR as a negative posttranscriptional modulator in inflammation. Mol. Cell 19, 777-789 (2005
97. Yu, C. et al. An essential function of the SRC-3 coactivator in suppression of cytokine mRNA translation and inflammatory response. Mol. Cell 25, 765-778 (2007
98. Dixon, D.A. et al. Regulation of cyclooxygenase-2 expression by the translational silencer TIA-1. J. Exp. Med. 198, 475-481 (2003
99. Dhamija, S. et al. Interleukin-17 (IL-17) and IL-1 activate translation of overlapping sets of mRNAs, including that of the negative regulator of inflammation, MCPIP1. J. Biol. Chem. 288, 19250-19259 (2013
100. Yamamoto, M. et al. Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein IκBζ. Nature 430, 218-222 (2004
101. Chang, C.H. et al. Posttranscriptional control of T cell effector function by aerobic glycolysis. Cell 153, 1239-1251 (2013
102. Warner, J.R., Knopf, P.M. & Rich, A. A multiple ribosomal structure in protein synthesis. Proc. Natl. Acad. Sci. USA 49, 122-129 (1963
103. Johannes, G., Carter, M.S., Eisen, M.B., Brown, P.O. & Sarnow, P. Identification of eukaryotic mRNAs that are translated at reduced cap binding complex eIF4F concentrations using a cDNA microarray. Proc. Natl. Acad. Sci. USA 96, 13118-13123 (1999
104. Karginov, F.V. & Hannon, G.J. Remodeling of Ago2-mRNA interactions upon cellular stress reflects miRNA complementarity and correlates with altered translation rates. Genes Dev. 27, 1624-1632 (2013
105. Ingolia, N.T., Ghaemmaghami, S., Newman, J.R. & Weissman, J.S. Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324, 218-223 (2009
106. Ingolia, N.T., Brar, G.A., Rouskin, S., McGeachy, A.M. & Weissman, J.S. The ribosome profiling strategy for monitoring translation in vivo by deep sequencing of ribosome-protected mRNA fragments. Nat. Protoc. 7, 1534-1550 (2012
107. Zoschke, R., Watkins, K.P. & Barkan, A. A rapid ribosome profiling method elucidates chloroplast ribosome behavior in vivo. Plant Cell 25, 2265-2275 (2013
108. Larsson, O., Sonenberg, N. & Nadon, R. Identification of differential translation in genome wide studies. Proc. Natl. Acad. Sci. USA 107, 21487-21492 (2010
109. Olshen, A.B. et al. Assessing gene-level translational control from ribosome profiling. Bioinformatics 29, 2995-3002 (2013
110. Larsson, O & Nadon, R. Re-Analysis of genome wide data on mammalian microRNA-mediated suppression of gene expression. Translation 1, 1-9 (2013
111. Eliseeva, I.A., Vorontsov, I.E., Babeyev, K.E., Buyanova, S.M., Sysoeva, M.A. & Kondrashov, F.A. et al. In silico motif analysis suggests an interplay of transcriptional and translational control in mTOR response. Translation 1, 1-7 (2013
112. Larsson, O., Sonenberg, N. & Nadon, R. Anota: Analysis of differential translation in genome-wide studies. Bioinformatics 27, 1440-1441 (2011
113. Colman, H. et al. Genome-wide analysis of host mRNA translation during hepatitis C virus infection. J. Virol. 87, 6668-6677 (2013
114. Larsson, O. et al. Distinct perturbation of the translatome by the antidiabetic drug metformin. Proc. Natl. Acad. Sci. USA 109, 8977-8982 (2012
115. Parker, M.W. et al. Fibrotic extracellular matrix activates a profibrotic positive feedback loop. J. Clin. Invest. 124, 1622-1635 (2014
116. Stumpf, C.R., Moreno, M.V., Olshen, A.B., Taylor, B.S. & Ruggero, D. The translational landscape of the mammalian cell cycle. Mol. Cell 52, 574-582 (2013
117. Tebaldi, T., Dassi, E., Kostoska, G., Viero, G. & Quattrone, A. tRanslatome: An R/Bioconductor package to portray translational control. Bioinformatics 30, 289-291 (2014
118. Michel, A.M. et al. GWIPS-viz: Development of a ribo-seq genome browser. Nucleic Acids Res. 42, D859-D864 (2014
119. Schneider-Poetsch, T. et al. Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat. Chem. Biol. 6, 209-217 (2010
120. Lee, S. et al. Global mapping of translation initiation sites in mammalian cells at single-nucleotide resolution. Proc. Natl. Acad. Sci. USA 109, E2424-E2432 (2012
121. Ingolia, N.T., Lareau, L.F. & Weissman, J.S. Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of Mammalian proteomes. Cell 147, 789-802 (2011
122. Guttman, M., Russell, P., Ingolia, N.T., Weissman, J.S. & Lander, E.S. Ribosome profiling provides evidence that large noncoding RNAs do not encode proteins. Cell 154, 240-251 (2013
123. Fresno, M., Jimenez, A. & Vazquez, D. Inhibition of translation in eukaryotic systems by harringtonine. Eur. J. Biochem. 72, 323-330 (1977
124. Larsson, O. et al. Eukaryotic translation initiation factor 4E induced progression of primary human mammary epithelial cells along the cancer pathway is associated with targeted translational deregulation of oncogenic drivers and inhibitors. Cancer Res. 67, 6814-6824 (2007
125. Mamane, Y. et al. Epigenetic activation of a subset of mRNAs by eIF4E explains its effects on cell proliferation. PLoS ONE 2, e242 (2007
126. Rajasekhar, V.K. et al. Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes. Mol. Cell 12, 889-901 (2003
127. Tominaga, Y., Tamguney, T., Kolesnichenko, M., Bilanges, B. & Stokoe, D. Translational deregulation in PDK-1-/- embryonic stem cells. Mol. Cell. Biol. 25, 8465-8475 (2005
128. Mikulits, W. et al. Isolation of translationally controlled mRNAs by differential screening. FASEB J. 14, 1641-1652 (2000
129. Grolleau, A. et al. Global and specific translational control by rapamycin in T cells uncovered by microarrays and proteomics. J. Biol. Chem. 277, 22175-22184 (2002
130. Ceppi, M. et al. Ribosomal protein mRNAs are translationally-regulated during human dendritic cells activation by LPS. Immunome Res. 5, 5 (2009
131. Kitamura, H. et al. Genome-wide identification and characterization of transcripts translationally regulated by bacterial lipopolysaccharide in macrophage-like J774.1 cells. Physiol. Genomics 33, 121-132 (2008
132. Ring, A.M. et al. Mechanistic and structural insight into the functional dichotomy between IL-2 and IL-15. Nat. Immunol. 13, 1187-1195 (2012