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Translational control in cancer

Silvera, Deborah, Formenti, Silvia C., Schneider, Robert J.·2010·Nature Reviews Cancer
DOI 10.1038/nrc2824
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  1. Pianese, G. Beitrag zur histologie und Aetiologie der carcinoma histologische und experimentelle. Beitr. Pathol. Anat. Allgem. Pathol. 142, 1–193 (1896).
  2. Gani, R. The nucleoli of cultured human lymphocytes. I. Nucleolar morphology in relation to transformation and the DNA cycle. Exp. Cell Res. 97, 249–258 (1976). · DOI
  3. Johnson, L. F., Levis, R., Abelson, H. T., Green, H. & Penman, S. Changes in RNA in relation to growth of the fibroblast. IV. Alterations in theproduction and processing of mRNA and rRNA in resting and growing cells. J. Cell Biol. 71, 933–938 (1976). · DOI
  4. Zetterberg, A., Larsson, O. & Wiman, K. G. What is the restriction point? Curr. Opin. Cell. Biol. 7, 835–842 (1995). · DOI · Paper page
  5. Barna, M. et al. Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency. Nature 456, 971–975 (2008). This paper directly links Myc overexpression to cancer development through alteration of translational control. MYC reduces IRES-dependent Cdk11 translation during mitosis and increases chromosome instability. · DOI · Paper page
  6. Getz, M. J., Elder, P. K., Benz, E. W. Jr, Stephens, R. E. & Moses, H. L. Effect of cell proliferation on levels and diversity of poly(A)-containing mRNA. Cell 7, 255–265 (1976). · DOI
  7. Connolly, E., Braunstein, S., Formenti, S. & Schneider, R. J. Hypoxia inhibits protein synthesis through a 4E-BP1 and elongation factor 2 kinase pathway controlled by mTOR and uncoupled in breast cancer cells. Mol. Cell. Biol. 26, 3955–3965 (2006). · DOI
  8. Wek, R. C., Jiang, H. Y. & Anthony, T. G. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans. 34, 7–11 (2006). · DOI · Paper page
  9. Donze, O., Jagus, R., Koromilas, A. E., Hershey, J. W. & Sonenberg, N. Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells. EMBO J. 14, 3828–3834 (1995). · DOI · Paper page
  10. Koromilas, A. E., Roy, S., Barber, G. N., Katze, M. G. & Sonenberg, N. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257, 1685–1689 (1992). · DOI · Paper page
  11. Tejada, S. et al. Eukaryotic initiation factors (eIF) 2α and 4E expression, localization, and phosphorylation in brain tumors. J. Histochem. Cytochem. 57, 503–512 (2009). · DOI
  12. Abraham, N. et al. Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR. J. Biol. Chem. 274, 5953–5962 (1999). · DOI
  13. Yang, Y. L. et al. Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinase. EMBO J. 14, 6095–6106 (1995). · DOI · Paper page
  14. Bi, M. et al. ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth. EMBO J. 24, 3470–3481 (2005). · DOI · Paper page
  15. Koritzinsky, M. et al. Gene expression during acute and prolonged hypoxia is regulated by distinct mechanisms of translational control. EMBO J. 25, 1114–1125 (2006). · DOI · Paper page
  16. Schewe, D. M. & Aguirre-Ghiso, J. A. Inhibition of eIF2α dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy. Cancer Res. 69, 1545–1552 (2009). · DOI
  17. Dong, Z. & Zhang, J. T. Initiation factor eIF3 and regulation of mRNA translation, cell growth, and cancer. Crit. Rev. Oncol. Hematol. 59, 169–180 (2006). · DOI · Paper page
  18. Zhang, L., Pan, X. & Hershey, J. W. Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells. J. Biol. Chem. 282, 5790–5800 (2007). · DOI · Paper page
  19. Dong, Z., Liu, L. H., Han, B., Pincheira, R. & Zhang, J. T. Role of eIF3 p170 in controlling synthesis of ribonucleotide reductase M2 and cell growth. Oncogene 23, 3790–3801 (2004). · DOI
  20. Dong, Z. & Zhang, J. T. EIF3 p170, a mediator of mimosine effect on protein synthesis and cell cycle progression. Mol. Biol. Cell 14, 3942–3951 (2003). · doi:10.1091/mbc.e02-12-0784
  21. Scoles, D. R., Yong, W. H., Qin, Y., Wawrowsky, K. & Pulst, S. M. Schwannomin inhibits tumorigenesis through direct interaction with the eukaryotic initiation factor subunit c (eIF3c). Hum. Mol. Genet. 15, 1059–1070 (2006). · DOI
  22. Nupponen, N. N. et al. Amplification and overexpression of p40 subunit of eukaryotic translation initiation factor 3 in breast and prostate cancer. Am. J. Pathol. 154, 1777–1783 (1999). · DOI
  23. Saramaki, O. et al. Amplification of EIF3S3 gene is associated with advanced stage in prostate cancer. Am. J. Pathol. 159, 2089–2094 (2001). · DOI
  24. Cappuzzo, F. et al. MYC and EIF3H coamplification significantly improve response and survival of non-small cell lung cancer patients (NSCLC) treated with gefitinib. J. Thorac Oncol. 4, 472–478 (2009). · DOI
  25. Shi, J. et al. Decreased expression of eukaryotic initiation factor 3f deregulates translation and apoptosis in tumor cells. Oncogene 25, 4923–4936 (2006). · DOI
  26. Marchetti, A. et al. Int-6, a highly conserved, widely expressed gene, is mutated by mouse mammary tumor virus in mammary preneoplasia. J. Virol. 69, 1932–1938 (1995). This paper remains the clearest example of transformation by a retrovirus that alters translational control. It shows that MMTV inserts within EIf3e (also known as Int6 ) to truncate its expression and induce mammary tumorigenesis in the mouse. · DOI
  27. Rasmussen, S. B., Kordon, E., Callahan, R. & Smith, G. H. Evidence for the transforming activity of a truncated Int6 gene, in vitro. Oncogene 20, 5291–5301 (2001). · DOI
  28. Mayeur, G. L. & Hershey, J. W. Malignant transformation by the eukaryotic translation initiation factor 3 subunit p48 (eIF3e). FEBS Lett. 514, 49–54 (2002). · doi:10.1016/s0014-5793(02)02307-4
  29. Mack, D. L., Boulanger, C. A., Callahan, R. & Smith, G. H. Expression of truncated Int6/eIF3e in mammary alveolar epithelium leads to persistent hyperplasia and tumorigenesis. Breast Cancer Res. 9, R42 (2007). · DOI
  30. Marchetti, A., Buttitta, F., Pellegrini, S., Bertacca, G. & Callahan, R. Reduced expression of INT-6/eIF3-p48 in human tumors. Int. J. Oncol. 18, 175–179 (2001).
  31. Umar, A. et al. Identification of a putative protein profile associating with tamoxifen therapy-resistance in breast cancer. Mol. Cell. Proteomics 8, 1278–1294 (2009). · DOI
  32. Zanelli, C. F. & Valentini, S. R. Is there a role for eIF5A in translation? Amino Acids 33, 351–358 (2007). · doi:10.1007/s00726-007-0533-0
  33. Jenkins, Z. A., Haag, P. G. & Johansson, H. E. Human eIF5A2 on chromosome 3q25-q27 is a phylogenetically conserved vertebrate variant of eukaryotic translation initiation factor 5A with tissue-specific expression. Genomics 71, 101–109 (2001). · doi:10.1006/geno.2000.6418
  34. Benne, R., Brown-Luedi, M. L. & Hershey, J. W. Purification and characterization of protein synthesis initiation factors eIF-1, eIF-4C, eIF-4D, and eIF-5 from rabbit reticulocytes. J. Biol. Chem. 253, 3070–3077 (1978). · doi:10.1016/s0021-9258(17)40804-0
  35. Kemper, W. M., Berry, K. W. & Merrick, W. C. Purification and properties of rabbit reticulocyte protein synthesis initiation factors M2Bα and M2Bβ. J. Biol. Chem. 251, 5551–5557 (1976). · doi:10.1016/s0021-9258(17)33095-8
  36. Saini, P., Eyler, D. E., Green, R. & Dever, T. E. Hypusine-containing protein eIF5A promotes translation elongation. Nature 459, 118–121 (2009). · DOI · Paper page
  37. Guan, X. Y. et al. Oncogenic role of eIF-5A2 in the development of ovarian cancer. Cancer Res. 64, 4197–4200 (2004). · DOI
  38. Zender, L. et al. An oncogenomics-based in vivo RNAi screen identifies tumor suppressors in liver cancer. Cell 135, 852–864 (2008). · DOI · Paper page
  39. Hanauske-Abel, H. M. et al. Detection of a sub-set of polysomal mRNAs associated with modulation of hypusine formation at the G1-S boundary. Proposal of a role for eIF-5A in onset of DNA replication. FEBS Lett. 366, 92–98 (1995). · doi:10.1016/0014-5793(95)00493-s
  40. Cracchiolo, B. M. et al. Eukaryotic initiation factor 5A-1 (eIF5A-1) as a diagnostic marker for aberrant proliferation in intraepithelial neoplasia of the vulva. Gynecol. Oncol. 94, 217–222 (2004). · doi:10.1016/j.ygyno.2004.03.018
  41. Balabanov, S. et al. Hypusination of eukaryotic initiation factor 5A (eIF5A): a novel therapeutic target in BCR-ABL-positive leukemias identified by a proteomics approach. Blood 109, 1701–1711 (2007). · DOI
  42. Miluzio, A., Beugnet, A., Volta, V. & Biffo, S. Eukaryotic initiation factor 6 mediates a continuum between 60S ribosome biogenesis and translation. EMBO Rep. 10, 459–465 (2009). · DOI
  43. Rosso, P. et al. Overexpression of p27BBP in head and neck carcinomas and their lymph node metastases. Head Neck 26, 408–417 (2004). · doi:10.1002/hed.10401
  44. Sanvito, F. et al. Expression of a highly conserved protein, p27BBP, during the progression of human colorectal cancer. Cancer Res. 60, 510–516 (2000).
  45. Flavin, R. J. et al. Altered eIF6 and Dicer expression is associated with clinicopathological features in ovarian serous carcinoma patients. Mod. Pathol. 21, 676–684 (2008). · DOI
  46. Gandin, V. et al. Eukaryotic initiation factor 6 is rate-limiting in translation, growth and transformation. Nature 455, 684–688 (2008). This paper expanded the understanding of the role of protein synthesis in cancer to include regulation of the 60S ribosome subunit and its ability to form translation-capable 80S ribosomes through external signals acting on eIF6. · DOI
  47. Sonenberg, N. & Hinnebusch, A. G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136, 731–745 (2009). · DOI · Paper page
  48. Graff, J. R., Konicek, B. W., Carter, J. H. & Marcusson, E. G. Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res. 68, 631–634 (2008). · DOI · Paper page
  49. Lazaris-Karatzas, A., Montine, K. S. & Sonenberg, N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345, 544–547 (1990). · DOI · Paper page
  50. 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. 12, 1234–1238 (1992).
  51. Lazaris-Karatzas, A. et al. Ras mediates translation initiation factor 4E-induced malignant transformation. Genes Dev. 6, 1631–1642 (1992). The first study to clearly identify a translation factor (eIF4E) as an effector of an oncogenic pathway. It showed that eIF4E overexpression, as occurs in many cancers, is stimulated by the Ras pathway, and is an essential partner in tumorigenesis through increased translation. · DOI
  52. Ruggero, D. et al. The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nature Med. 10, 484–486 (2004). · DOI · Paper page
  53. Wendel, H. G. et al. Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 428, 332–337 (2004). · DOI · Paper page
  54. Koromilas, A. E., Lazaris-Karatzas, A. & Sonenberg, N. mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. EMBO J. 11, 4153–4158 (1992). · DOI · Paper page
  55. Rosenwald, I. B., Rhoads, D. B., Callanan, L. D., Isselbacher, K. J. & Schmidt, E. V. Increased expression of eukaryotic translation initiation factors eIF-4E and eIF-2α in response to growth induction by c-myc. Proc. Natl. Acad. Sci. USA 90, 6175–6178 (1993). · DOI · Paper page
  56. Mamane, Y. et al. Epigenetic activation of a subset of mRNAs by eIF4E explains its effects on cell proliferation. PLoS One 2, e242 (2007). · DOI · Paper page
  57. 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). · DOI · Paper page
  58. Schneider, R. J. & Sonenberg, N. in Translational Control in Biology and Medicine (eds. Mathews, M. B., Sonenberg, N. & Hershey, J. W. B.) (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 2007).
  59. Waskiewicz, A. J. et al. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell. Biol. 19, 1871–1880 (1999). · DOI · Paper page
  60. Kim, S. H., Miller, F. R., Tait, L., Zheng, J. & Novak, R. F. Proteomic and phosphoproteomic alterations in benign, premalignant and tumor human breast epithelial cells and xenograft lesions: biomarkers of progression. Int. J. Cancer 124, 2813–2828 (2009). · DOI
  61. Graff, J. R. et al. eIF4E activation is commonly elevated in advanced human prostate cancers and significantly related to reduced patient survival. Cancer Res. 69, 3866–3873 (2009). · DOI · Paper page
  62. Rahmani, M., Davis, E. M., Bauer, C., Dent, P. & Grant, S. Apoptosis induced by the kinase inhibitor BAY 43–9006 in human leukemia cells involves down-regulation of Mcl-1 through inhibition of translation. J. Biol. Chem. 280, 35217–35227 (2005). · DOI · Paper page
  63. Liu, L. et al. Sorafenib blocks the RAF/MEK/ERK pathway, inhibits tumor angiogenesis, and induces tumor cell apoptosis in hepatocellular carcinoma model PLC/PRF/5. Cancer Res. 66, 11851–11858 (2006). · DOI · Paper page
  64. Noske, A. et al. Activation of mTOR in a subgroup of ovarian carcinomas: correlation with p-eIF-4E and prognosis. Oncol. Rep. 20, 1409–1417 (2008).
  65. Fan, S. et al. Phosphorylated eukaryotic translation initiation factor 4 (eIF4E) is elevated in human cancer tissues. Cancer Biol. Ther. 8, 1463–1469 (2009). · DOI
  66. Coleman, L. J. et al. Combined analysis of eIF4E and 4E-binding protein expression predicts breast cancer survival and estimates eIF4E activity. Br. J. Cancer 100, 1393–1399 (2009). · DOI
  67. Salehi, Z. & Mashayekhi, F. Expression of the eukaryotic translation initiation factor 4E (eIF4E) and 4E-BP1 in esophageal cancer. Clin. Biochem. 39, 404–409 (2006). · DOI
  68. Braunstein, S. et al. A hypoxia-controlled cap-dependent to cap-independent translation switch in breast cancer. Mol. Cell 28, 501–512 (2007). This study showed that most LABCs overexpress eIF4G1 and 4E-BP1, which was shown in animal models to comprise a hypoxia-activated switch that stimulates IRES-dependent translation of survival, angiogenesis and hypoxia-orchestrating mRNAs, promoting development of locally advanced tumours. · DOI · Paper page
  69. Fukuchi-Shimogori, T. et al. Malignant transformation by overproduction of translation initiation factor eIF4G. Cancer Res. 57, 5041–5044 (1997).
  70. Comtesse, N. et al. Frequent overexpression of the genes FXR1, CLAPM1 and EIF4G located on amplicon 3q26–27 in squamous cell carcinoma of the lung. Int. J. Cancer 120, 2538–2544 (2007). · DOI
  71. Bauer, C. et al. Translation initiation factor eIF-4G is immunogenic, overexpressed, and amplified in patients with squamous cell lung carcinoma. Cancer 92, 822–829 (2001). · doi:10.1002/1097-0142(20010815)92:4<822::aid-cncr1388>3.0.co;2-a
  72. Rosenwald, I. B., Hutzler, M. J., Wang, S., Savas, L. & Fraire, A. E. Expression of eukaryotic translation initiation factors 4E and 2α is increased frequently in bronchioloalveolar but not in squamous cell carcinomas of the lung. Cancer 92, 2164–2171 (2001). · doi:10.1002/1097-0142(20011015)92:8<2164::aid-cncr1559>3.0.co;2-a
  73. Silvera, D. et al. Essential role for eIF4GI overexpression in the pathogenesis of inflammatory breast cancer. Naure Cell Biol. 11, 903–908 (2009). This paper showed that overexpression of eIF4G1 occurs in IBC and is crucial for disease development. High levels of eIF4G1 promoted IRES-dependent translation of P120CTN and formation of metastatic emboli.
  74. Silvera, D. & Schneider, R. J. Inflammatory breast cancer cells are constitutively adapted to hypoxia. Cell Cycle 8, 3091–3096 (2009). · DOI
  75. Shuda, M. et al. Enhanced expression of translation factor mRNAs in hepatocellular carcinoma. Anticancer Res. 20, 2489–2494 (2000).
  76. Eberle, J., Krasagakis, K. & Orfanos, C. E. Translation initiation factor eIF-4A1 mRNA is consistently overexpressed in human melanoma cells in vitro. Int. J. Cancer 71, 396–401 (1997). · doi:10.1002/(sici)1097-0215(19970502)71:3<396::aid-ijc16>3.0.co;2-e
  77. Bordeleau, M. E. et al. Therapeutic suppression of translation initiation modulates chemosensitivity in a mouse lymphoma model. J. Clin. Invest. 118, 2651–2660 (2008). This study used small-molecule library screening to identify a specific inhibitor of eIF4A (silvestrol), demonstrating that initiation factors could be targeted for anticancer therapy. Silvestrol enhanced chemosensitivity in a mouse lymphoma model.
  78. Lankat-Buttgereit, B. & Goke, R. The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation. Biol. Cell 101, 309–317 (2009). · DOI · Paper page
  79. LaRonde-LeBlanc, N., Santhanam, A. N., Baker, A. R., Wlodawer, A. & Colburn, N. H. Structural basis for inhibition of translation by the tumor suppressor Pdcd4. Mol. Cell. Biol. 27, 147–156 (2007). · DOI
  80. Holcik, M. Targeting translation for treatment of cancer—a novel role for IRES? Curr. Cancer Drug Targets. 4, 299–311 (2004). · DOI
  81. Jopling, C. L. & Willis, A. E. N. -myc translation is initiated via an internal ribosome entry segment that displays enhanced activity in neuronal cells. Oncogene 20, 2664–26670 (2001). · DOI
  82. Spriggs, K. A. et al. Canonical initiation factor requirements of the Myc family of internal ribosome entry segments. Mol. Cell. Biol. 29, 1565–1574 (2009). · DOI
  83. Chappell, S. A. et al. A mutation in the c-myc-IRES leads to enhanced internal ribosome entry in multiple myeloma: a novel mechanism of oncogene de-regulation. Oncogene 19, 4437–4440 (2000). · DOI
  84. Evans, J. R. et al. Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo. Oncogene 22, 8012–8020 (2003). · DOI · Paper page
  85. Shi, Y. et al. IL-6-induced stimulation of c-myc translation in multiple myeloma cells is mediated by myc internal ribosome entry site function and the RNA-binding protein, hnRNP A1. Cancer Res. 68, 10215–10222 (2008). · DOI
  86. Holcik, M., Yeh, C., Korneluk, R. G. & Chow, T. Translational upregulation of X-linked inhibitor of apoptosis (XIAP) increases resistance to radiation induced cell death. Oncogene 19, 4174–4177 (2000). · DOI · Paper page
  87. Desplanques, G. et al. Impact of XIAP protein levels on the survival of myeloma cells. Haematologica 94, 87–93 (2009). · DOI
  88. Ma, X. M. & Blenis, J. Molecular mechanisms of mTOR-mediated translational control. Nature Rev. Mol. Cell. Biol. 10, 307–318 (2009). · DOI · Paper page
  89. 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). · DOI · Paper page
  90. Pyronnet, S. et al. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J. 18, 270–279 (1999). This study demonstrated that MNK1 is part of the eIF4F complex, resides on initiation factor eIF4G and phosphorylates eIF4E after assembly of eIF4F to promote translation initiation. · DOI · Paper page
  91. Guertin, D. A. & Sabatini, D. M. Defining the role of mTOR in cancer. Cancer Cell 12, 9–22 (2007). · DOI · Paper page
  92. Lin, C. J., Malina, A. & Pelletier, J. c-Myc and eIF4F constitute a feedforward loop that regulates cell growth: implications for anticancer therapy. Cancer Res. 69, 7491–7494 (2009). · DOI
  93. Mavrakis, K. J. et al. Tumorigenic activity and therapeutic inhibition of Rheb GTPase. Genes Dev. 22, 2178–2188 (2008). This study demonstrated that RHEB, an activator of mTOR in the mTORC1 complex, promotes lymphoma in PTEN-deficient mice and requires eIF4E as an effector. · DOI
  94. Wu, X., Senechal, K., Neshat, M. S., Whang, Y. E. & Sawyers, C. L. The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway. Proc. Natl. Acad. Sci. USA 95, 15587–15591 (1998). · DOI · Paper page
  95. Zhou, X. et al. Activation of the Akt/mammalian target of rapamycin/4E-BP1 pathway by ErbB2 overexpression predicts tumor progression in breast cancers. Clin. Cancer Res. 10, 6779–6788 (2004). · DOI · Paper page
  96. Ruggero, D. & Pandolfi, P. P. Does the ribosome translate cancer? Nature Rev. Cancer 3, 179–192 (2003). · DOI · Paper page
  97. Nakamura, J. L., Garcia, E. & Pieper, R. O. S6K1 plays a key role in glial transformation. Cancer Res. 68, 6516–6523 (2008). · DOI
  98. Holz, M. K., Ballif, B. A., Gygi, S. P. & Blenis, J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123, 569–580 (2005). · DOI · Paper page
  99. Dorrello, N. V. et al. S6K1- and βTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth. Science 314, 467–471 (2006). This paper showed that eIF4A is a target of the tumour suppressor PDCD4. In response to mitogens, S6K1 phosphorylates PDCD4, which is then rapidly degraded in the proteasome, releasing eIF4A activity and promoting translation. · DOI · Paper page
  100. Carayol, N. et al. Suppression of programmed cell death 4 (PDCD4) protein expression by BCR-ABL-regulated engagement of the mTOR/p70 S6 kinase pathway. J. Biol. Chem. 283, 8601–8610 (2008). · DOI
  101. Shahbazian, D. et al. The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity. EMBO J. 25, 2781–2791 (2006). · DOI · Paper page
  102. Maira, S. M., Stauffer, F., Schnell, C. & Garcia-Echeverria, C. PI3K inhibitors for cancer treatment: where do we stand? Biochem. Soc. Trans. 37, 265–272 (2009). · DOI
  103. Choo, A. Y. & Blenis, J. Not all substrates are treated equally: implications for mTOR, rapamycin-resistance and cancer therapy. Cell Cycle 8, 567–572 (2009). · DOI
  104. Yu, K. 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. 70, 621–631 (2010). · DOI · Paper page
  105. Feldman, M. E. et al. Active-site inhibitors of mTOR target rapamycin-resistant outputs of mTORC1 and mTORC2. PLoS Biol. 7, e38 (2009). · DOI · Paper page
  106. Avruch, J. et al. Activation of mTORC1 in two steps: Rheb-GTP activation of catalytic function and increased binding of substrates to raptor. Biochem. Soc. Trans. 37, 223–226 (2009). · DOI
  107. Vander Haar, E., Lee, S. I., Bandhakavi, S., Griffin, T. J. & Kim, D. H. Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40. Nature Cell Biol. 9, 316–323 (2007). · DOI · Paper page
  108. Madhunapantula, S. V., Sharma, A. & Robertson, G. P. PRAS40 deregulates apoptosis in malignant melanoma. Cancer Res. 67, 3626–3636 (2007). · DOI
  109. Johnson, M. D., O'Connell, M., Vito, F. & Bakos, R. S. Increased STAT-3 and synchronous activation of Raf-1-MEK-1-MAPK, and phosphatidylinositol 3-Kinase-Akt-mTOR pathways in atypical and anaplastic meningiomas. J. Neurooncol. 92, 129–136 (2009). · DOI
  110. Kwiatkowski, D. J. Tuberous sclerosis: from tubers to mTOR. Ann. Hum. Genet. 67, 87–96 (2003). · DOI · Paper page
  111. Braunstein, S., Badura, M. L., Xi, Q., Formenti, S. C. & Schneider, R. J. Regulation of protein synthesis by ionizing radiation. Mol. Cell. Biol. 29, 5645–5656 (2009). · DOI
  112. Haines, G. K. 3rd. et al. Expression of the double-stranded RNA-dependent protein kinase (p68) in squamous cell carcinoma of the head and neck region. Arch. Otolaryngol. Head Neck Surg. 119, 1142–1147 (1993). · DOI
  113. Haines, G. K. et al. Correlation of the expression of double-stranded RNA-dependent protein kinase (p68) with differentiation in head and neck squamous cell carcinoma. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 63, 289–295 (1993). · doi:10.1007/bf02899275
  114. Haines, G. K. 3rd. et al. Interferon-responsive protein kinase (p68) and proliferating cell nuclear antigen are inversely distributed in head and neck squamous cell carcinoma. Tumour Biol. 19, 52–59 (1998). · DOI
  115. Terada, T., Maeta, H., Endo, K. & Ohta, T. Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: correlations with histologic types, pathologic parameters, and Ki-67 labeling. Hum. Pathol. 31, 817–821 (2000). · DOI
  116. Kim, S. H., Forman, A. P., Mathews, M. B. & Gunnery, S. Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR. Oncogene 19, 3086–3094 (2000). · DOI
  117. Haines, G. K. et al. Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues. Tumour Biol. 17, 5–12 (1996). · DOI
  118. Shimada, A. et al. Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma. Cancer Res. 58, 4434–4438 (1998).
  119. Rosenwald, I. B., Wang, S., Savas, L., Woda, B. & Pullman, J. Expression of translation initiation factor eIF-2α is increased in benign and malignant melanocytic and colonic epithelial neoplasms. Cancer 98, 1080–1088 (2003). · doi:10.1002/cncr.11619
  120. Wang, S. et al. Expression of eukaryotic translation initiation factors 4E and 2α correlates with the progression of thyroid carcinoma. Thyroid 11, 1101–1107 (2001). · DOI
  121. Wang, S. et al. Expression of the eukaryotic translation initiation factors 4E and 2α in non-Hodgkin's lymphomas. Am. J. Pathol. 155, 247–255 (1999). · doi:10.1016/s0002-9440(10)65118-8
  122. Rosenwald, I. B. et al. Expression of the translation initiation factors eIF-4E and eIF-2* is frequently increased in neoplastic cells of Hodgkin lymphoma. Hum. Pathol. 39, 910–916 (2008). · doi:10.1016/j.humpath.2007.10.021
  123. Bachmann, F., Banziger, R. & Burger, M. M. Cloning of a novel protein overexpressed in human mammary carcinoma. Cancer Res. 57, 988–994 (1997).
  124. Dellas, A. et al. Expression of p150 in cervical neoplasia and its potential value in predicting survival. Cancer 83, 1376–1383 (1998). · doi:10.1002/(sici)1097-0142(19981001)83:7<1376::aid-cncr15>3.0.co;2-1
  125. Pincheira, R., Chen, Q. & Zhang, J. T. Identification of a 170-kDa protein over-expressed in lung cancers. Br. J. Cancer 84, 1520–1527 (2001). · doi:10.1054/bjoc.2001.1828
  126. Chen, G. & Burger, M. M. p150 expression and its prognostic value in squamous-cell carcinoma of the esophagus. Int. J. Cancer 84, 95–100 (1999).
  127. Chen, G. & Burger, M. M. p150 overexpression in gastric carcinoma: the association with p53, apoptosis and cell proliferation. Int. J. Cancer 112, 393–398 (2004). · doi:10.1002/ijc.20443
  128. Rothe, M., Ko, Y., Albers, P. & Wernert, N. Eukaryotic initiation factor 3 p110 mRNA is overexpressed in testicular seminomas. Am. J. Pathol. 157, 1597–1604 (2000). · doi:10.1016/s0002-9440(10)64797-9
  129. Guan, X. Y. et al. Isolation of a novel candidate oncogene within a frequently amplified region at 3q26 in ovarian cancer. Cancer Res. 61, 3806–3809 (2001).
  130. Xie, D. et al. Overexpression of EIF-5A2 is associated with metastasis of human colorectal carcinoma. Hum. Pathol. 39, 80–86 (2008). · doi:10.1016/j.humpath.2007.05.011
  131. Luo, J. H. et al. Overexpression of EIF-5A2 predicts tumor recurrence and progression in pTa/pT1 urothelial carcinoma of the bladder. Cancer Sci. 100, 896–902 (2009). · doi:10.1111/j.1349-7006.2009.01126.x
  132. Chen, W. et al. Overexpression of EIF-5A2 is an independent predictor of outcome in patients of urothelial carcinoma of the bladder treated with radical cystectomy. Cancer Epidemiol. Biomarkers Prev. 18, 400–408 (2009). · doi:10.1158/1055-9965.epi-08-0754
  133. De Benedetti, A. & Graff, J. R. eIF-4E expression and its role in malignancies and metastases. Oncogene 23, 3189–3199 (2004). · DOI · Paper page
  134. Thumma, S. C. & Kratzke, R. A. Translational control: a target for cancer therapy. Cancer Lett. 258, 1–8 (2007). · DOI
  135. Bauer, C. et al. Overexpression of the eukaryotic translation initiation factor 4G (eIF4G-1) in squamous cell lung carcinoma. Int. J. Cancer 98, 181–185 (2002). · DOI
  136. Brass, N. et al. Translation initiation factor eIF-4γ is encoded by an amplified gene and induces an immune response in squamous cell lung carcinoma. Hum. Mol. Genet. 6, 33–39 (1997). · DOI
  137. Konicek, B. W., Dumstorf, C. A. & Graff, J. R. Targeting the eIF4F translation initiation complex for cancer therapy. Cell Cycle 7, 2466–2471 (2008). · DOI
  138. Moerke, N. J. et al. Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell 128, 257–267 (2007). · DOI · Paper page
  139. Tamburini, J. et al. Protein synthesis is resistant to rapamycin and constitutes a promising therapeutic target in acute myeloid leukemia. Blood 114, 1618–1627 (2009). · DOI · Paper page
  140. Faivre, S., Kroemer, G. & Raymond, E. Current development of mTOR inhibitors as anticancer agents. Nature Rev. Drug Discov. 5, 671–688 (2006). · DOI · Paper page

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Metadata

Authors
Silvera, D., Formenti, S. C., & Schneider, R. J.
Venue
Nature Reviews Cancer
Publisher
Springer Science and Business Media LLC
Published
2010-04
Volume
10
Issue
4
Pages
254-266
ISSN
  • 1474-175X (ISSN-L)
  • 1474-1768
DOI
10.1038/nrc2824
OpenAlex
W2089716875
Cited by
821
References
8
FWCI
3.45
Type
journal article
Language
en
Open access
closed
Licence

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Silvera, D., Formenti, S. C., & Schneider, R. J. (2010). Translational control in cancer. Nature Reviews Cancer. https://doi.org/10.1038/nrc2824

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