Eukaryotic translation initiation factor 4E as a novel therapeutic target in hematological malignancies and beyond

Bibliography

• Spilka R, Ernst C, Mehta AK, et al. Eukaryotic translation initiation factors in cancer development and progression. Cancer Lett 2013;340(1):9-21
   PubMed Web of Science ®Google Scholar
• Gingras AC, Raught B, Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 1999;68:913-63
   PubMed Web of Science ®Google Scholar
• Sonenberg N. eIF4E, the mRNA cap-binding protein: from basic discovery to translational research. Biochem Cell Biol 2008;86(2):178-83
   Google Scholar
• Lejbkowicz F, Goyer C, Darveau A, et al. A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc Natl Acad Sci USA 1992;89(20):9612-16
   PubMed Web of Science ®Google Scholar
• Strudwick S, Borden KL. The emerging roles of translation factor eIF4E in the nucleus. Differentiation 2002;70(1):10-22
   Google Scholar
• Lazaris-Karatzas A, Smith MR, Frederickson RM, et al. Ras mediates translation initiation factor 4E-induced malignant transformation. Genes Dev 1992;6(9):1631-42
   Google Scholar
• Lazaris-Karatzas A, Sonenberg N. The mRNA 5’ cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformation of primary rodent fibroblasts. Mol Cell Biol 1992;12(3):1234-8
   PubMedGoogle Scholar
• Lazaris-Karatzas A, Montine KS, Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5’ cap. Nature 1990;345(6275):544-7
   PubMed Web of Science ®Google Scholar
• Larsson O, Li S, Issaenko OA, 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 2007;67(14):6814-24
   PubMed Web of Science ®Google Scholar
• Avdulov S, Li S, Michalek V, 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 2004;5(6):553-63
   PubMed Web of Science ®Google Scholar
• Graff J, Boghaert E, De Benedetti A, et al. Reduction of translation initiation factor 4E decreases the malignancy of ras-transformed cloned rat embryo fibroblasts. Int J Cancer 1995;60(2):255-63
   Google Scholar
• Ruggero D, Montanaro L, Ma L, et al. The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nat Med 2004;10(5):484-6
   PubMed Web of Science ®Google Scholar
• Wendel HG, De Stanchina E, Fridman JS, et al. Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 2004;428(6980):332-7
   PubMed Web of Science ®Google Scholar
• Graff JR, Konicek BW, Carter JH, et al. Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res 2008;68(3):631-4
   PubMed Web of Science ®Google Scholar
• Hsieh AC, Ruggero D. Targeting eIF4E in Cancer. Clin Cancer Res 2010;16(20):4914-20
   Google Scholar
• Montanaro L, Pandolfi PP. Initiation of mRNA translation in oncogenesis: the role of eIF4E. Cell Cycle 2004;3(11):1387-9
   PubMed Web of Science ®Google Scholar
• Culjkovic B, Borden KL. Understanding and targeting the eukaryotic translation initiation factor eIF4E in head and neck cancer. J Oncol 2009;2009:981679
   PubMedGoogle Scholar
• Tamburini J, Green AS, Chapuis N, et al. Targeting translation in acute myeloid leukemia: a new paradigm for therapy? Cell Cycle 2009;8(23):3893-9
   PubMed Web of Science ®Google Scholar
• Flowers A, Chu QD, Panu L, et al. Eukaryotic initiation factor 4E overexpression in triple-negative breast cancer predicts a worse outcome. Surgery 2009;146(2):220-6
   Google Scholar
• Meric-Bernstam F, Chen H, Akcakanat A, et al. Aberrations in translational regulation are associated with poor prognosis in hormone receptor-positive breast cancer. Breast Cancer Res 2012;14(5):R138
   PubMed Web of Science ®Google Scholar
• Li BD, McDonald JC, Nassar R, et al. Clinical outcome in stage I to III breast carcinoma and eIF4E overexpression. Ann Surg 1998;227(5):756-6l; discussion 761-3
   Google Scholar
• Sunavala-Dossabhoy G, Palaniyandi S, Clark C, et al. Analysis of eIF4E and 4EBP1 mRNAs in head and neck cancer. Laryngoscope 2011;121(10):2136-41
   Google Scholar
• Nathan CO, Franklin S, Abreo FW, et al. Analysis of surgical margins with the molecular marker eIF4E: a prognostic factor in patients with head and neck cancer. J Clin Oncol 1999;17(9):2909-14
   Google Scholar
• Nathan CO, Liu L, Li BD, et al. Detection of the proto-oncogene eIF4E in surgical margins may predict recurrence in head and neck cancer. Oncogene 1997;15(5):579-84
   PubMed Web of Science ®Google Scholar
• Crew JP, Fuggle S, Bicknell R, et al. Eukaryotic initiation factor-4E in superficial and muscle invasive bladder cancer and its correlation with vascular endothelial growth factor expression and tumour progression. Br J Cancer 2000;82(1):161-6
   PubMed Web of Science ®Google Scholar
• Graff JR, Konicek BW, Lynch RL, et al. eIF4E activation is commonly elevated in advanced human prostate cancers and significantly related to reduced patient survival. Cancer Res 2009;69(9):3866-73
   PubMed Web of Science ®Google Scholar
• Seki N, Takasu T, Sawada S, et al. Prognostic significance of expression of eukaryotic initiation factor 4E and 4E binding protein 1 in patients with pathological stage I invasive lung adenocarcinoma. Lung Cancer 2010;70(3):329-34
   PubMed Web of Science ®Google Scholar
• Dong K, Wang R, Wang X, et al. Tumor-specific RNAi targeting eIF4E suppresses tumor growth, induces apoptosis and enhances cisplatin cytotoxicity in human breast carcinoma cells. Breast Cancer Res Treat 2009;113(3):443-56
   Google Scholar
• Soni A, Akcakanat A, Singh G, et al. eIF4E knockdown decreases breast cancer cell growth without activating Akt signaling. Mol Cancer Ther 2008;7(7):1782-8
   PubMedGoogle Scholar
• Graff JR, Konicek BW, Vincent TM, et al. Therapeutic suppression of translation initiation factor eIF4E expression reduces tumor growth without toxicity. J Clin Invest 2007;117(9):2638-48
   PubMed Web of Science ®Google Scholar
• Borden KLB. Targeting the oncogene eIF4E in cancer: from the bench to clinical trials, in Clinical and Investigative Medicine (Online). Canadian Society for Clinical Investigation; Ottawa: 2011. p. 5
   Google Scholar
• Iborra FJ, Jackson DA, Cook PR. Coupled transcription and translation within nuclei of mammalian cells. Science 2001;293(5532):1139-42
   PubMed Web of Science ®Google Scholar
• Culjkovic-Kraljacic B, Baguet A, Volpon L, et al. The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation. Cell Rep 2012;2(2):207-15
   PubMed Web of Science ®Google Scholar
• Culjkovic B, Topisirovic I, Skrabanek L, et al. eIF4E promotes nuclear export of cyclin D1 mRNAs via an element in the 3’UTR. J Cell Biol 2005;169(2):245-56
   PubMed Web of Science ®Google Scholar
• Culjkovic B, Topisirovic I, Skrabanek L, et al. eIF4E is a central node of an RNA regulon that governs cellular proliferation. J Cell Biol 2006;175(3):415-26
   PubMed Web of Science ®Google Scholar
• Lin CJ, Cencic R, Mills JR, et al. c-Myc and eIF4F are components of a feedforward loop that links transcription and translation. Cancer Res 2008;68(13):5326-34
   Google Scholar
• Labisso WL, Wirth M, Stojanovic N, et al. MYC directs transcription of MCL1 and eIF4E genes to control sensitivity of gastric cancer cells toward HDAC inhibitors. Cell Cycle 2012;11(8):1593-602
   PubMed Web of Science ®Google Scholar
• Jones RM, Branda J, Johnston KA, et al. An essential E box in the promoter of the gene encoding the mRNA cap-binding protein (eukaryotic initiation factor 4E) is a target for activation by c-myc. Mol Cell Biol 1996;16(9):4754-64
   PubMedGoogle Scholar
• Hariri F, Arguello M, Volpon L, et al. The eukaryotic translation initiation factor eIF4E is a direct transcriptional target of NF-κB and is aberrantly regulated in acute myeloid leukemia. Leukemia 2013;27(10):2047-55
   Google Scholar
• Yi T, Papadopoulos E, Hagner PR, et al. Hypoxia-inducible factor-1alpha (HIF-1alpha) promotes cap-dependent translation of selective mRNAs through up-regulating initiation factor eIF4E1 in breast cancer cells under hypoxia conditions. J Biol Chem 2013;288(26):18732-42
   Google Scholar
• Sorrells DL, Black DR, Meschonat C, et al. Detection of eIF4E gene amplification in breast cancer by competitive PCR. Ann Surg Oncol 1998;5(3):232-7
   Google Scholar
• Sorrells DL, Ghali GE, Meschonat C, et al. Competitive PCR to detect eIF4E gene amplification in head and neck cancer. Head Neck 1999;21(1):60-5
   Google Scholar
• Sorrells DL, Meschonat C, Black D, et al. Pattern of amplification and overexpression of the eukaryotic initiation factor 4E gene in solid tumor. J Surg Res 1999;85(1):37-42
   PubMed Web of Science ®Google Scholar
• Topisirovic I, Siddiqui N, Orolicki S, et al. Stability of eukaryotic translation initiation factor 4E mRNA is regulated by HuR, and this activity is dysregulated in cancer. Mol Cell Biol 2009;29(5):1152-62
   PubMedGoogle Scholar
• Richter JD, Sonenberg N. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 2005;433(7025):477-80
   PubMed Web of Science ®Google Scholar
• Cohen N, Sharma M, Kentsis A, et al. PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA. EMBO J 2001;20(16):4547-59
   PubMed Web of Science ®Google Scholar
• Topisirovic I, Borden KL. Homeodomain proteins and eukaryotic translation initiation factor 4E (eIF4E): an unexpected relationship. Histol Histopathol 2005;20(4):1275-84
   PubMed Web of Science ®Google Scholar
• Gingras AC, Kennedy SG, O’Leary MA, et al. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway. Genes Dev 1998;12(4):502-13
   PubMed Web of Science ®Google Scholar
• Brunn GJ, Hudson CC, Sekulic A, et al. Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin. Science 1997;277(5322):99-101
   PubMed Web of Science ®Google Scholar
• Korkolopoulou P, Levidou G, El-Habr EA, et al. Phosphorylated 4E-binding protein 1 (p-4E-BP1): a novel prognostic marker in human astrocytomas. Histopathology 2012;61(2):293-305
   PubMedGoogle Scholar
• Yeh CJ, Chuang WY, Chao YK, et al. High expression of phosphorylated 4E-binding protein 1 is an adverse prognostic factor in esophageal squamous cell carcinoma. Virchows Arch 2011;458(2):171-8
   Google Scholar
• Armengol G, Rojo F, Castellvi J, et al. 4E-binding protein 1: a key molecular "funnel factor" in human cancer with clinical implications. Cancer Res 2007;67(16):7551-5
   PubMed Web of Science ®Google Scholar
• Wang X, Flynn A, Waskiewicz AJ, et al. The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways. J Biol Chem 1998;273(16):9373-7
   PubMed Web of Science ®Google Scholar
• Pyronnet S, Imataka H, Gingras AC, et al. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J 1999;18(1):270-9
   PubMed Web of Science ®Google Scholar
• Ueda T, Sasaki M, Elia AJ, et al. Combined deficiency for MAP kinase-interacting kinase 1 and 2 (Mnk1 and Mnk2) delays tumor development. Proc Natl Acad Sci USA 2010;107(32):13984-90
   PubMed Web of Science ®Google Scholar
• Furic L, Rong L, Larsson O, et al. eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression. Proc Natl Acad Sci USA 2010;107(32):14134-9
   PubMed Web of Science ®Google Scholar
• Silva RLA, Wendel HG. MNK, EIF4E and targeting translation for therapy. Cell Cycle 2008;7(5):553-5
   PubMed Web of Science ®Google Scholar
• Topisirovic I, Ruiz-Gutierrez M, Borden KL. Phosphorylation of the eukaryotic translation initiation factor eIF4E contributes to its transformation and mRNA transport activities. Cancer Res 2004;64(23):8639-42
   PubMed Web of Science ®Google Scholar
• De Benedetti A, Graff J. eIF-4E expression and its role in malignancies and metastases. Oncogene 2004;23(18):3189-99
   PubMed Web of Science ®Google Scholar
• Wang S, Rosenwald IB, Hutzler MJ, et al. Expression of the eukaryotic translation initiation factors 4E and 2alpha in non-Hodgkin’s lymphomas. Am J Pathol 1999;155(1):247-55
   PubMed Web of Science ®Google Scholar
• Kodali D, Rawal A, Ninan MJ, et al. Expression and phosphorylation of eukaryotic translation initiation factor 4E binding protein 1 in B-cell lymphomas and reactive lymphoid tissues. Arch Pathol Lab Med 2011;135(3):365-71
   Google Scholar
• Topisirovic I, Guzman M, McConnell M, et al. Aberrant eukaryotic translation initiation factor 4E-dependent mRNA transport impedes hematopoietic differentiation and contributes to leukemogenesis. Mol Cell Biol 2003;23(24):8992-9002
   PubMed Web of Science ®Google Scholar
• Kentsis A, Topisirovic I, Culjkovic B, et al. Ribavirin suppresses eIF4E-mediated oncogenic transformation by physical mimicry of the 7-methyl guanosine mRNA cap. Proc Natl Acad Sci USA 2004;101(52):18105-10
   PubMed Web of Science ®Google Scholar
• Assouline S, Culjkovic B, Cocolakis E, et al. Molecular targeting of the oncogene eIF4E in acute myeloid leukemia (AML): a proof-of-principle clinical trial with ribavirin. Blood 2009;114(2):257-60
   PubMed Web of Science ®Google Scholar
• Lim S, Saw TY, Zhang M, et al. Targeting of the MNK-eIF4E axis in blast crisis chronic myeloid leukemia inhibits leukemia stem cell function. Proc Natl Acad Sci USA 2013;110(25):E2298-307
   PubMed Web of Science ®Google Scholar
• Altman JK, Szilard A, Konicek BW, et al. Inhibition of Mnk kinase activity by cercosporamide and suppressive effects on acute myeloid leukemia precursors. Blood 2013;121(18):3675-81
   PubMed Web of Science ®Google Scholar
• Martinez-Marignac V, Shawi M, Pinedo-Carpio E, et al. Pharmacological targeting of eIF4E in primary CLL lymphocytes. Blood Cancer J 2013;3:e146
   PubMedGoogle Scholar
• Altman JK, Sassano A, Platanias LC. Targeting mTOR for the treatment of AML. New agents and new directions. Oncotarget 2011;2(6):510-17
   PubMedGoogle Scholar
• Davids MS, Brown JR. Targeting the B cell receptor pathway in chronic lymphocytic leukemia. Leuk Lymphoma 2012;53(12):2362-70
   PubMed Web of Science ®Google Scholar
• Fruman DA, Rommel C. PI3K and cancer: lessons, challenges and opportunities. Nat Rev Drug Discov 2014;13(2):140-56
   PubMed Web of Science ®Google Scholar
• Kelly KR, Rowe JH, Padmanabhan S, et al. Mammalian target of rapamycin as a target in hematological malignancies. Target Oncol 2011;6(1):53-61
   Google Scholar
• Martelli AM, Evangelisti C, Chappell W, et al. Targeting the translational apparatus to improve leukemia therapy: roles of the PI3K/PTEN/Akt/mTOR pathway. Leukemia 2011;25(7):1064-79
   PubMed Web of Science ®Google Scholar
• O’Reilly KE, Rojo F, She QB, et al. mTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt. Cancer Res 2006;66(3):1500-8
   PubMed Web of Science ®Google Scholar
• Hsieh AC, Costa M, Zollo O, et al. Genetic dissection of the oncogenic mTOR pathway reveals druggable addiction to translational control via 4EBP-eIF4E. Cancer Cell 2010;17(3):249-61
   PubMed Web of Science ®Google Scholar
• Sun SY, Rosenberg LM, Wang X, et al. Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition. Cancer Res 2005;65(16):7052-8
   PubMed Web of Science ®Google Scholar
• Ilic N, Utermark T, Widlund HR, et al. PI3K-targeted therapy can be evaded by gene amplification along the MYC-eukaryotic translation initiation factor 4E (eIF4E) axis. Proc Natl Acad Sci USA 2011;108(37):E699-708
   PubMed Web of Science ®Google Scholar
• De Benedetti A, Graff JR. eIF-4E expression and its role in malignancies and metastases. Oncogene 2004;23(18):3189-99
   PubMed Web of Science ®Google Scholar
• Silvera D, Formenti SC, Schneider RJ. Translational control in cancer. Nat Rev Cancer 2010;10(4):254-66
   PubMed Web of Science ®Google Scholar
• Rosenwald IB, Chen JJ, Wang S, et al. Upregulation of protein synthesis initiation factor eIF-4E is an early event during colon carcinogenesis. Oncogene 1999;18(15):2507-17
   PubMed Web of Science ®Google Scholar
• Kleiner HE, Krishnan P, Tubbs J, et al. Tissue microarray analysis of eIF4E and its downstream effector proteins in human breast cancer. J Exp Clin Cancer Res 2009;28:5
   PubMed Web of Science ®Google Scholar
• Yang SX, Hewitt SM, Steinberg SM, et al. Expression levels of eIF4E, VEGF, and cyclin D1, and correlation of eIF4E with VEGF and cyclin D1 in multi-tumor tissue microarray. Oncol Rep 2007;17(2):281-7
   Google Scholar
• Khoury T, Alrawi S, Ramnath N, et al. Eukaryotic initiation factor-4E and cyclin D1 expression associated with patient survival in lung cancer. Clin Lung Cancer 2009;10(1):58-66
   PubMed Web of Science ®Google Scholar
• Byrnes K, White S, Chu Q, et al. High eIF4E, VEGF, and microvessel density in stage I to III breast cancer. Ann Surg 2006;243(5):684-90; discussion 691-2
   Google Scholar
• Ramaswamy S, Ross KN, Lander ES, et al. A molecular signature of metastasis in primary solid tumors. Nat Genet 2003;33(1):49-54
   PubMed Web of Science ®Google Scholar
• Hsieh AC, Liu Y, Edlind MP, et al. The translational landscape of mTOR signalling steers cancer initiation and metastasis. Nature 2012;485(7396):55-61
   PubMed Web of Science ®Google Scholar
• 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 1997;16(8):1921-33
   PubMed Web of Science ®Google Scholar
• Waskiewicz AJ, Flynn A, Proud CG, et al. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J 1997;16(8):1909-20
   PubMed Web of Science ®Google Scholar
• Flynn A, Proud CG. 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 1995;270(37):21684-8
   PubMed Web of Science ®Google Scholar
• Waskiewicz AJ, Johnson JC, Penn B, et al. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol Cell Biol 1999;19(3):1871-80
   PubMed Web of Science ®Google Scholar
• Scheper GC, Morrice NA, Kleijn M, et al. 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. Mol Cell Biol 2001;21(3):743-54
   PubMed Web of Science ®Google Scholar
• Joshi B, Cai AL, Keiper BD, et al. Phosphorylation of eukaryotic protein synthesis initiation factor 4E at Ser-209. J Biol Chem 1995;270(24):14597-603
   Google Scholar
• Rhoads RE. Regulation of eukaryotic protein synthesis by initiation factors. J Biol Chem 1993;268(5):3017-20
   Google Scholar
• Kleijn M, Scheper GC, Voorma HO, et al. Regulation of translation initiation factors by signal transduction. Eur J Biochem 1998;253(3):531-44
   Google Scholar
• Raught B, Gingras AC. eIF4E activity is regulated at multiple levels. Int J Biochem Cell Biol 1999;31(1):43-57
   PubMed Web of Science ®Google Scholar
• Minich WB, Balasta ML, Goss DJ, et al. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc Natl Acad Sci USA 1994;91(16):7668-72
   Google Scholar
• Scheper GC, van Kollenburg B, Hu J, et al. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J Biol Chem 2002;277(5):3303-9
   PubMed Web of Science ®Google Scholar
• Morley SJ, McKendrick L. Involvement of stress-activated protein kinase and p38/RK mitogen-activated protein kinase signaling pathways in the enhanced phosphorylation of initiation factor 4E in NIH 3T3 cells. J Biol Chem 1997;272(28):17887-93
   Google Scholar
• Scheper GC, van Wijk R, Thomas AM. Regulation of the activity of eukaryotic initiation factors in stressed cells. Prog Mol Subcell Biol 2001;27:40-56
   Google Scholar
• Marcotrigiano J, Gingras AC, Sonenberg N, et al. Cocrystal structure of the messenger RNA 5’ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 1997;89(6):951-61
   PubMed Web of Science ®Google Scholar
• Zuberek J, Wyslouch-Cieszynska A, Niedzwiecka A, et al. Phosphorylation of eIF4E attenuates its interaction with mRNA 5’ cap analogs by electrostatic repulsion: intein-mediated protein ligation strategy to obtain phosphorylated protein. RNA 2003;9(1):52-61
   Google Scholar
• Lachance PE, Miron M, Raught B, et al. Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth. Mol Cell Biol 2002;22(6):1656-63
   PubMedGoogle Scholar
• Reiling JH, Doepfner KT, Hafen E, et al. Diet-dependent effects of the Drosophila Mnk1/Mnk2 homolog Lk6 on growth via eIF4E. Curr Biol 2005;15(1):24-30
   Google Scholar
• Wendel HG, Silva RL, Malina A, et al. Dissecting eIF4E action in tumorigenesis. Genes Dev 2007;21(24):3232-7
   PubMed Web of Science ®Google Scholar
• Fan S, Ramalingam S, Kauh J, et al. Phosphorylated eukaryotic translation initiation factor 4 (eIF4E) is elevated in human cancer tissues. Cancer Biol Ther 2009;8(15):1463-9
   PubMed Web of Science ®Google Scholar
• Adesso L, Calabretta S, Barbagallo F, et al. Gemcitabine triggers a pro-survival response in pancreatic cancer cells through activation of the MNK2/eIF4E pathway. Oncogene 2013;32(23):2848-57
   PubMed Web of Science ®Google Scholar
• Yoshizawa A, Fukuoka J, Shimizu S, et al. Overexpression of phospho-eIF4E is associated with survival through AKT pathway in non-small cell lung cancer. Clin Cancer Res 2010;16(1):240-8
   PubMed Web of Science ®Google Scholar
• Zheng J, Li J, Xu L, et al. Phosphorylated Mnk1 and eIF4E are associated with lymph node metastasis and poor prognosis of nasopharyngeal carcinoma. PLoS One 2014;9(2):e89220
   Google Scholar
• Polunovsky VA, Rosenwald IB, Tan AT, et al. Translational control of programmed cell death: eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc. Mol Cell Biol 1996;16(11):6573-81
   PubMedGoogle Scholar
• Li S, Takasu T, Perlman DM, et al. Translation factor eIF4E rescues cells from Myc-dependent apoptosis by inhibiting cytochrome c release. J Biol Chem 2003;278(5):3015-22
   PubMed Web of Science ®Google Scholar
• Vanharanta S, Massague J. Origins of metastatic traits. Cancer Cell 2013;24(4):410-21
   PubMed Web of Science ®Google Scholar
• Robichaud N, del Rincon S, Huor B, et al. Phosphorylation of eIF4E promotes EMT and metastasis via translational control of SNAIL and MMP-3. Oncogene 2014; doi: 10.1038/onc.2014.146
   PubMed Web of Science ®Google Scholar
• Kalluri R, Weinberg RA. The basics of epithelial-mesenchymal transition. J Clin Invest 2009;119(6):1420-8
   PubMed Web of Science ®Google Scholar
• Lochter A, Galosy S, Muschler J, et al. Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells. J Cell Biol 1997;139(7):1861-72
   PubMed Web of Science ®Google Scholar
• Lamouille S, Xu J, Derynck R. Molecular mechanisms of epithelial-mesenchymal transition. Nat Rev Mol Cell Biol 2014;15(3):178-96
   PubMed Web of Science ®Google Scholar
• Bakin AV, Rinehart C, Tomlinson AK, et al. p38 mitogen-activated protein kinase is required for TGFbeta-mediated fibroblastic transdifferentiation and cell migration. J Cell Sci 2002;115(Pt 15):3193-206
   PubMed Web of Science ®Google Scholar
• Gui T, Sun Y, Shimokado A, et al. The roles of mitogen-activated protein kinase pathways in TGF-beta-induced epithelial-mesenchymal transition. J Signal Transduct 2012;2012:289243
   PubMedGoogle Scholar
• Parvani JG, Taylor MA, Schiemann WP. Noncanonical TGF-beta signaling during mammary tumorigenesis. J Mammary Gland Biol Neoplasia 2011;16(2):127-46
   Google Scholar
• Zhou FF, Yan M, Guo GF, et al. Knockdown of eIF4E suppresses cell growth and migration, enhances chemosensitivity and correlates with increase in Bax/Bcl-2 ratio in triple-negative breast cancer cells. Med Oncol 2011;28(4):1302-7
   PubMed Web of Science ®Google Scholar
• Rinker-Schaeffer CW, Graff JR, De Benedetti A, et al. Decreasing the level of translation initiation factor 4E with antisense RNA causes reversal of ras-mediated transformation and tumorigenesis of cloned rat embryo fibroblasts. Int J Cancer 1993;55(5):841-7
   Web of Science ®Google Scholar
• Nasr Z, Robert F, Porco JA Jr, et al. eIF4F suppression in breast cancer affects maintenance and progression. Oncogene 2013;32(7):861-71
   Google Scholar
• De Benedetti A, Joshi-Barve S, Rinker-Schaeffer C, et al. Expression of antisense RNA against initiation factor eIF-4E mRNA in HeLa cells results in lengthened cell division times, diminished translation rates, and reduced levels of both eIF-4E and the p220 component of eIF-4F. Mol Cell Biol 1991;11(11):5435-45
   PubMedGoogle Scholar
• DeFatta RJ, Nathan CO, De Benedetti A. Antisense RNA to eIF4E suppresses oncogenic properties of a head and neck squamous cell carcinoma cell line. Laryngoscope 2000;110(6):928-33
   Google Scholar
• Oridate N, Kim HJ, Xu X, et al. Growth inhibition of head and neck squamous carcinoma cells by small interfering RNAs targeting eIF4E or cyclin D1 alone or combined with cisplatin. Cancer Biol Ther 2005;4(3):318-23
   PubMed Web of Science ®Google Scholar
• Hong DS, Kurzrock R, Oh Y, et al. A phase 1 dose escalation, pharmacokinetic, and pharmacodynamic evaluation of eIF-4E antisense oligonucleotide LY2275796 in patients with advanced cancer. Clin Cancer Res 2011;17(20):6582-91
   PubMed Web of Science ®Google Scholar
• Moerke NJ, Aktas H, Chen H, et al. Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell 2007;128(2):257-67
   PubMed Web of Science ®Google Scholar
• Tamburini J, Green AS, Bardet V, et al. Protein synthesis is resistant to rapamycin and constitutes a promising therapeutic target in acute myeloid leukemia. Blood 2009;114(8):1618-27
   PubMed Web of Science ®Google Scholar
• Chen L, Aktas BH, Wang Y, et al. Tumor suppression by small molecule inhibitors of translation initiation. Oncotarget 2012;3(8):869-81
   PubMed Web of Science ®Google Scholar
• Descamps G, Gomez-Bougie P et al. The cap-translation inhibitor 4EGI-1 induces apoptosis in multiple myeloma through Noxa induction. Br J Cancer 2012;106(10):1660-7
   Google Scholar
• Fan S, Li Y, Yue P, et al. The eIF4E/eIF4G interaction inhibitor 4EGI-1 augments TRAIL-mediated apoptosis through c-FLIP Down-regulation and DR5 induction independent of inhibition of cap-dependent protein translation. Neoplasia 2010;12(4):346-56
   Google Scholar
• Willimott S, Beck D, Ahearne MJ, et al. Cap-translation inhibitor, 4EGI-1, restores sensitivity to ABT-737 apoptosis through cap-dependent and -independent mechanisms in chronic lymphocytic leukemia. Clin Cancer Res 2013;19(12):3212-23
   PubMed Web of Science ®Google Scholar
• Takrouri K, Chen T, Papadopoulos E, et al. Structure-activity relationship study of 4EGI-1, small molecule eIF4E/eIF4G protein-protein interaction inhibitors. Eur J Med Chem 2014;77:361-77
   Google Scholar
• Yefidoff-Freedman R, Chen T, Sahoo R, et al. 3-substituted indazoles as configurationally locked 4EGI-1 mimetics and inhibitors of the eIF4E/eIF4G interaction. ChemBioChem 2014;15(4):595-611
   Google Scholar
• Ko SY, Guo H, Barengo N, et al. Inhibition of ovarian cancer growth by a tumor-targeting peptide that binds eukaryotic translation initiation factor 4E. Clin Cancer Res 2009;15(13):4336-47
   Google Scholar
• Knauf U, Tschopp C, Gram H. Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol Cell Biol 2001;21(16):5500-11
   PubMed Web of Science ®Google Scholar
• Bain J, Plater L, Elliott M, et al. The selectivity of protein kinase inhibitors: a further update. Biochem J 2007;408(3):297-315
   PubMed Web of Science ®Google Scholar
• Marzec M, Liu X, Wysocka M, et al. Simultaneous inhibition of mTOR-containing complex 1 (mTORC1) and MNK induces apoptosis of cutaneous T-cell lymphoma (CTCL) cells. PLoS One 2011;6(9):e24849
   PubMed Web of Science ®Google Scholar
• Wheater MJ, Johnson PW, Blaydes JP. The role of MNK proteins and eIF4E phosphorylation in breast cancer cell proliferation and survival. Cancer Biol Ther 2010;10(7):728-35
   PubMed Web of Science ®Google Scholar
• Zhang M, Fu W, Prabhu S, et al. Inhibition of polysome assembly enhances imatinib activity against chronic myelogenous leukemia and overcomes imatinib resistance. Mol Cell Biol 2008;28(20):6496-509
   PubMed Web of Science ®Google Scholar
• Bianchini A, Loiarro M, Bielli P, et al. Phosphorylation of eIF4E by MNKs supports protein synthesis, cell cycle progression and proliferation in prostate cancer cells. Carcinogenesis 2008;29(12):2279-88
   PubMed Web of Science ®Google Scholar
• Shi Y, Frost P, Hoang B, et al. MNK1-induced eIF-4E phosphorylation in myeloma cells: a pathway mediating IL-6-induced expansion and expression of genes involved in metabolic and proteotoxic responses. PLoS One 2014;9(4):e94011
   Google Scholar
• Grzmil M, Huber RM, Hess D, et al. MNK1 pathway activity maintains protein synthesis in rapalog-treated gliomas. J Clin Invest 2014;124(2):742-54
   PubMed Web of Science ®Google Scholar
• Konicek BW, Stephens JR, McNulty AM, et al. Therapeutic inhibition of MAP kinase interacting kinase blocks eukaryotic initiation factor 4E phosphorylation and suppresses outgrowth of experimental lung metastases. Cancer Res 2011;71(5):1849-57
   PubMed Web of Science ®Google Scholar
• Maimon A, Mogilevsky M, Shilo A, et al. Mnk2 alternative splicing modulates the p38-MAPK pathway and impacts Ras-induced transformation. Cell Rep 2014;7(2):501-13
   PubMed Web of Science ®Google Scholar
• Stead RL, Proud CG. Rapamycin enhances eIF4E phosphorylation by activating MAP kinase-interacting kinase 2a (Mnk2a). FEBS Lett 2013;587(16):2623-8
   PubMed Web of Science ®Google Scholar
• Diab S, Kumarasiri M, Yu M, et al. MAP kinase-interacting kinases-emerging targets against cancer. Chem Biol 2014;21(4):441-52
   Google Scholar
• Diab S, Teo T, Kumarasiri M, et al. Discovery of 5-(2-(phenylamino)pyrimidin-4-yl)thiazol-2(3H)-one derivatives as potent Mnk2 inhibitors: synthesis, SAR analysis and biological evaluation. ChemMedChem 2014;9(5):962-72
   PubMed Web of Science ®Google Scholar
• Ramalingam S, Gediya L, Kwegyir-Afful AK, et al. First MNKs degrading agents block phosphorylation of eIF4E, induce apoptosis, inhibit cell growth, migration and invasion in triple negative and Her2-overexpressing breast cancer cell lines. Oncotarget 2014;5(2):530-43
   PubMedGoogle Scholar
• Tan K, Culjkovic B, Amri A, et al. Ribavirin targets eIF4E dependent Akt survival signaling. Biochem Biophys Res Commun 2008;375(3):341-5
   Google Scholar
• Pettersson F, Yau C, Dobocan MC, et al. Ribavirin Treatment Effects on Breast Cancers Overexpressing eIF4E, a Biomarker with Prognostic Specificity for Luminal B-Type Breast Cancer. Clin Cancer Res 2011;17(9):2874-84
   PubMed Web of Science ®Google Scholar
• Kentsis A, Volpon L, Topisirovic I, et al. Further evidence that ribavirin interacts with eIF4E. RNA 2005;11(12):1762-6
   PubMed Web of Science ®Google Scholar
• Volpon L, Osborne MJ, Zahreddine H, et al. Conformational changes induced in the eukaryotic translation initiation factor eIF4E by a clinically relevant inhibitor, ribavirin triphosphate. Biochem Biophys Res Commun 2013;434(3):614-19
   PubMed Web of Science ®Google Scholar
• Kraljacic BC, Arguello M, Amri A, et al. Inhibition of eIF4E with ribavirin cooperates with common chemotherapies in primary acute myeloid leukemia specimens. Leukemia 2011;25(7):1197-200
   PubMed Web of Science ®Google Scholar
• Zahreddine HA, Culjkovic-Kraljacic B, Assouline S, et al. The sonic hedgehog factor Gli1 imparts drug resistance through inducible glucuronidation. Nature 2014; doi: 10.1038/nature13283
   Google Scholar
• Endres CJ, Moss AM, Govindarajan R, et al. The role of nucleoside transporters in the erythrocyte disposition and oral absorption of ribavirin in the wild-type and equilibrative nucleoside transporter 1(−/−) mice. J Pharmacol Exp Ther 2009;331(1):287-96
   PubMed Web of Science ®Google Scholar
• Endres CJ, Moss AM, Ke B, et al. The role of the equilibrative nucleoside transporter 1 (ENT1) in transport and metabolism of ribavirin by human and wild-type or Ent1-/- mouse erythrocytes. J Pharmacol Exp Ther 2009;329(1):387-98
   PubMed Web of Science ®Google Scholar
• Stanton BZ, Peng LF. Small-molecule modulators of the Sonic Hedgehog signaling pathway. Mol Biosyst 2010;6(1):44-54
   PubMedGoogle Scholar
• Choo AY, Yoon SO, Kim SG, et al. Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-type-specific repression of mRNA translation. Proc Natl Acad Sci USA 2008;105(45):17414-19
   PubMed Web of Science ®Google Scholar
• Feldman ME, Apsel B, Uotila A, et al. Active-site inhibitors of mTOR target rapamycin-resistant outputs of mTORC1 and mTORC2. PLoS Biol 2009;7(2):e38
   PubMed Web of Science ®Google Scholar
• Yu K, Shi C, Toral-Barza L, et al. Beyond rapalog therapy: preclinical pharmacology and antitumor activity of WYE-125132, an ATP-competitive and specific inhibitor of mTORC1 and mTORC2. Cancer Res 2010;70(2):621-31
   PubMed Web of Science ®Google Scholar
• Thoreen CC, Chantranupong L, Keys HR, et al. A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 2012;485(7396):109-13
   PubMed Web of Science ®Google Scholar
• De Benedetti A, Rhoads RE. Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology. Proc Natl Acad Sci USA 1990;87(21):8212-16
   Google Scholar
• Smith MR, Jaramillo M, Liu YL, et al. Translation initiation factors induce DNA synthesis and transform NIH 3T3 cells. New Biol 1990;2(7):648-54
   PubMedGoogle Scholar
• Rousseau D, Gingras AC, Pause A, et al. The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 1996;13(11):2415-20
   Google Scholar
• Yanagiya A, Suyama E, Adachi H, et al. Translational homeostasis via the mRNA cap-binding protein, eIF4E. Mol Cell 2012;46(6):847-58
   Google Scholar
• Alain T, Morita M, Fonseca BD, et al. eIF4E/4E-BP ratio predicts the efficacy of mTOR targeted therapies. Cancer Res 2012;72(24):6468-76
   PubMed Web of Science ®Google Scholar
• Shveygert M, Kaiser C, Bradrick SS, et al. Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by mitogen-activated protein kinase occurs through modulation of Mnk1-eIF4G interaction. Mol Cell Biol 2010;30(21):5160-7
   PubMed Web of Science ®Google Scholar
• Hall C, Dumstorf C, Konicek B, et al. eIF4E phosphorylation is Mnk-dependent but does not require assembly of the eIF4F translation initiation complex. In Proceedings of the 105th Annual Meeting of the American Association for Cancer Research; San Diego, CA: AACR 2014
   Google Scholar
• Jacobson BA, Thumma SC, Jay-Dixon J, et al. Targeting eukaryotic translation in mesothelioma cells with an eIF4E-specific antisense oligonucleotide. PLoS One 2013;8(11):e81669
   Google Scholar