Eukaryotic translation initiation factors in cancer development and progression

Cancer Letters

Volumn 340, Issue 1, 2013, Pages 9-21

  Spilka, Rita ^a,b   Ernst, Christina ^a   Mehta, Anita Kuldeep ^a   Haybaeck, Johannes ^a  

^a MEDICAL UNIVERSITY OF GRAZ   (Austria)

^b Hospital Zams   (Austria)

Author keywords

Cancer; Eukaryotic initiation factors; Translation initiation

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 1; INITIATION FACTOR 2; INITIATION FACTOR 3; INITIATION FACTOR 3A; INITIATION FACTOR 3B; INITIATION FACTOR 3C; INITIATION FACTOR 3D; INITIATION FACTOR 3E; INITIATION FACTOR 3F; INITIATION FACTOR 3G; INITIATION FACTOR 3H; INITIATION FACTOR 3I; INITIATION FACTOR 3J; INITIATION FACTOR 3K; INITIATION FACTOR 3L; INITIATION FACTOR 3M; INITIATION FACTOR 4; INITIATION FACTOR 4A; INITIATION FACTOR 4B; INITIATION FACTOR 4E; INITIATION FACTOR 4F; INITIATION FACTOR 4G; INITIATION FACTOR 5; INITIATION FACTOR 6; UNCLASSIFIED DRUG;

APOPTOSIS; CANCER GROWTH; CARCINOGENESIS; EUKARYOTE; GENE EXPRESSION; HUMAN; MALIGNANT TRANSFORMATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN RNA BINDING; SHORT SURVEY; SIGNAL TRANSDUCTION; TRANSLATION INITIATION; TUMOR VASCULARIZATION;

EUKARYOTA;

EID: 84883828800     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2013.06.019     Document Type: Review

References (166)

1. Silvera D., Arju R., Darvishian F., Levine P.H., Zolfaghari L., Goldberg J., Hochman T., Formenti S.C., Schneider R.J. Essential role for eIF4GI overexpression in the pathogenesis of inflammatory breast cancer. Nat. Cell Biol. 2009, 11:903-908.
2. 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 2010, 11:113-127.
3. Ganoza M.C., Kiel M.C., Aoki H. Evolutionary conservation of reactions in translation. Microbiology and molecular biology reviews: MMBR 2002, 66:460-485. (table of contents).
4. Kapp L.D., Lorsch J.R. The molecular mechanics of eukaryotic translation. Annu. Rev. Biochem. 2004, 73:657-704.
5. Saletta F., Suryo Rahmanto Y., Richardson D.R. The translational regulator eIF3a: the tricky eIF3 subunit!. Biochim. Biophys. Acta 1806, 2010:275-286.
6. De Benedetti A., Graff J.R. EIF-4E expression and its role in malignancies and metastases. Oncogene 2004, 23:3189-3199.
7. Dong Z., Zhang J.T. Initiation factor eIF3 and regulation of mRNA translation, cell growth, and cancer. Crit. Rev. Oncol./Hematol. 2006, 59:169-180.
8. Kyrpides N.C., Woese C.R. Universally conserved translation initiation factors. Proc. Nat. Acad. Sci. USA 1998, 95:224-228.
9. Fletcher C.M., Pestova T.V., Hellen C.U., Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J. 1999, 18:2631-2637.
10. Pestova T.V., Borukhov S.I., Hellen C.U. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 1998, 394:854-859.
11. Miyasaka H., Endo S., Shimizu H. Eukaryotic translation initiation factor 1 (eIF1), the inspector of good AUG context for translation initiation, has an extremely bad AUG context. J. Biosci. Bioeng. 2010, 109:635-637.
12. Yoon H.J., Donahue T.F. The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon. Mol. Cell. Biol. 1992, 12:248-260.
13. Sheikh M.S., Fornace A.J. Regulation of translation initiation following stress. Oncogene 1999, 18:6121-6128.
14. Reibarkh M., Yamamoto Y., Singh C.R., del Rio F., Fahmy A., Lee B., Luna R.E., Ii M., Wagner G., Asano K. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J. Biol. Chem. 2008, 283:1094-1103.
15. Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.M., Polakiewicz R.D., Comb M.J. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 2005, 23:94-101.
16. Fenner B.J., Scannell M., Prehn J.H. Expanding the substantial interactome of NEMO using protein microarrays. PLoS One 2010, 5:e8799.
17. Sudhakar A., Ramachandran A., Ghosh S., Hasnain S.E., Kaufman R.J., Ramaiah K.V. Phosphorylation of serine 51 in initiation factor 2 alpha (eIF2 alpha) promotes complex formation between eIF2 alpha(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B. Biochemistry 2000, 39:12929-12938.
18. Sattlegger E., Hinnebusch A.G. Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells. EMBO J. 2000, 19:6622-6633.
19. Krishnamoorthy J., Mounir Z., Raven J.F., Koromilas A.E. The eIF2alpha kinases inhibit vesicular stomatitis virus replication independently of eIF2alpha phosphorylation. Cell Cycle 2008, 7:2346-2351.
20. Harding H.P., Zhang Y., Bertolotti A., Zeng H., Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 2000, 5:897-904.
21. Pavitt G.D., Yang W., Hinnebusch A.G. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol. 1997, 17:1298-1313.
22. Dev K., Santangelo T.J., Rothenburg S., Neculai D., Dey M., Sicheri F., Dever T.E., Reeve J.N., Hinnebusch A.G. Archaeal aIF2B interacts with eukaryotic translation initiation factors eIF2alpha and eIF2Balpha: implications for aIF2B function and eIF2B regulation. J. Mol. Biol. 2009, 392:701-722.
23. Saito A., Ochiai K., Kondo S., Tsumagari K., Murakami T., Cavener D.R., Imaizumi K. Endoplasmic reticulum stress response mediated by the PERK-eIF2(alpha)-ATF4 pathway is involved in osteoblast differentiation induced by BMP2. J. Biol. Chem 2011, 286:4809-4818.
24. 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. 1995, 14:3828-3834.
25. Wang S., Rosenwald I.B., Hutzler M.J., Pihan G.A., Savas L., Chen J.J., Woda B.A. Expression of the eukaryotic translation initiation factors 4E and 2alpha in non-Hodgkin's lymphomas. Am. J. Pathol. 1999, 155:247-255.
26. Lam N., Sandberg M.L., Sugden B. High physiological levels of LMP1 result in phosphorylation of eIF2 alpha in Epstein-Barr virus-infected cells. J. Virol. 2004, 78:1657-1664.
27. Lobo M.V., Martin M.E., Perez M.I., Alonso F.J., Redondo C., Alvarez M.I., Salinas M. Levels, phosphorylation status and cellular localization of translational factor eIF2 in gastrointestinal carcinomas. Histochem. J. 2000, 32:139-150.
28. Rosenwald I.B., Hutzler M.J., Wang S., Savas L., Fraire A.E. Expression of eukaryotic translation initiation factors 4E and 2alpha is increased frequently in bronchioloalveolar but not in squamous cell carcinomas of the lung. Cancer 2001, 92:2164-2171.
29. Rosenwald I.B., Wang S., Savas L., Woda B., Pullman J. Expression of translation initiation factor eIF-2alpha is increased in benign and malignant melanocytic and colonic epithelial neoplasms. Cancer 2003, 98:1080-1088.
30. Pestova T.V., Hellen C.U. The structure and function of initiation factors in eukaryotic protein synthesis. Cell. Mol. Life Sci.: CMLS 2000, 57:651-674.
31. Dong Z., Liu Z., Cui P., Pincheira R., Yang Y., Liu J., Zhang J.T. Role of eIF3a in regulating cell cycle progression. Exp. Cell Res. 2009, 315:1889-1894.
32. Masutani M., Sonenberg N., Yokoyama S., Imataka H. Reconstitution reveals the functional core of mammalian eIF3. EMBO J. 2007, 26:3373-3383.
33. Fitzgerald K.D., Semler B.L. Bridging IRES elements in mRNAs to the eukaryotic translation apparatus. Biochim. Biophys. Acta 2009, 1789:518-528.
34. Benne R., Hershey J.W. Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes. Proc. Nat. Acad. Sci. USA 1976, 73:3005-3009.
35. Methot N., Song M.S., Sonenberg N. A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol. Cell. Biol. 1996, 16:5328-5334.
36. 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 2004, 23:3790-3801.
37. Bachmann F., Banziger R., Burger M.M. Cloning of a novel protein overexpressed in human mammary carcinoma. Cancer Res. 1997, 57:988-994.
38. Haybaeck J., O'Connor T., Spilka R., Spizzo G., Ensinger C., Mikuz G., Brunhuber T., Vogetseder A., Theurl I., Salvenmoser W., Draxl H., Banziger R., Bachmann F., Schafer G., Burger M., Obrist P. Overexpression of p150, a part of the large subunit of the eukaryotic translation initiation factor 3, in colon cancer. Anticancer Res 2010, 30:1047-1055.
39. Pincheira R., Chen Q., Zhang J.T. Identification of a 170-kDa protein over-expressed in lung cancers. Br. J. Cancer 2001, 84:1520-1527.
40. Chen G., Burger M.M. P150 overexpression in gastric carcinoma: the association with p53, apoptosis and cell proliferation. Int. J. Can. J. Int. du Can. 2004, 112:393-398.
41. Dellas A., Torhorst J., Bachmann F., Banziger R., Schultheiss E., Burger M.M. Expression of p150 in cervical neoplasia and its potential value in predicting survival. Cancer 1998, 83:1376-1383.
42. Xu T.R., Lu R.F., Romano D., Pitt A., Houslay M.D., Milligan G., Kolch W. Eukaryotic translation initiation factor 3, subunit a, regulates the extracellular signal-regulated kinase pathway. Mol. Cell. Biol. 2012, 32:88-95.
43. Wang Z., Chen J., Sun J., Cui Z., Wu H. RNA interference-mediated silencing of eukaryotic translation initiation factor 3, subunit B (EIF3B) gene expression inhibits proliferation of colon cancer cells. World J. Surg. Oncol. 2012, 10:119.
44. Loftus B.J., Kim U.J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Deslattes Mays A., Cao Y., Xu R.X., Kang H.L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D. Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics 1999, 60:295-308.
45. Rauch J., Ahlemann M., Schaffrik M., Mack B., Ertongur S., Andratschke M., Zeidler R., Lang S., Gires O. Allogenic antibody-mediated identification of head and neck cancer antigens. Biochem. Biophys. Res. Commun. 2004, 323:156-162.
46. Rothe M., Ko Y., Albers P., Wernert N. Eukaryotic initiation factor 3 p110 mRNA is overexpressed in testicular seminomas. Am. J. Pathol. 2000, 157:1597-1604.
47. 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. 2006, 15:1059-1070.
48. Kim H.K., Choi I.J., Kim C.G., Kim H.S., Oshima A., Michalowski A., Green J.E. A gene expression signature of acquired chemoresistance to cisplatin and fluorouracil combination chemotherapy in gastric cancer patients. PLoS ONE 2011, 6:e16694.
49. Marchetti A., Buttitta F., Miyazaki S., Gallahan D., Smith G.H., Callahan R. Int-6, a highly conserved, widely expressed gene, is mutated by mouse mammary tumor virus in mammary preneoplasia. J. Virol. 1995, 69:1932-1938.
50. Rasmussen S.B., Kordon E., Callahan R., Smith G.H. Evidence for the transforming activity of a truncated Int6 gene, in vitro. Oncogene 2001, 20:5291-5301.
51. Mayeur G.L., Hershey J.W. Malignant transformation by the eukaryotic translation initiation factor 3 subunit p48 (eIF3e). FEBS Lett. 2002, 514:49-54.
52. Marchetti A., Buttitta F., Pellegrini S., Bertacca G., Callahan R. Reduced expression of INT-6/eIF3-p48 in human tumors. Int. J. Oncol. 2001, 18:175-179.
53. Miyazaki S., Imatani A., Ballard L., Marchetti A., Buttitta F., Albertsen H., Nevanlinna H.A., Gallahan D., Callahan R. The chromosome location of the human homolog of the mouse mammary tumor-associated gene INT6 and its status in human breast carcinomas. Genomics 1997, 46:155-158.
54. Traicoff J.L., Chung J.Y., Braunschweig T., Mazo I., Shu Y., Ramesh A., D'Amico M.W., Galperin M.M., Knezevic V., Hewitt S.M. Expression of EIF3-p48/INT6, TID1 and Patched in cancer, a profiling of multiple tumor types and correlation of expression. J. Biomed. Sci. 2007, 14:395-405.
55. Buttitta F., Martella C., Barassi F., Felicioni L., Salvatore S., Rosini S., D'Antuono T., Chella A., Mucilli F., Sacco R., Mezzetti A., Cuccurullo F., Callahan R., Marchetti A. Int6 expression can predict survival in early-stage non-small cell lung cancer patients. Clin. Can. Res.: An Off. J. Am. Assoc. Can. Res. 2005, 11:3198-3204.
56. Doldan A., Chandramouli A., Shanas R., Bhattacharyya A., Cunningham J.T., Nelson M.A., Shi J. Loss of the eukaryotic initiation factor 3f in pancreatic cancer. Mol. Carcinog. 2008, 47:235-244.
57. Doldan A., Chandramouli A., Shanas R., Bhattacharyya A., Leong S.P., Nelson M.A., Shi J. Loss of the eukaryotic initiation factor 3f in melanoma. Mol. Carcinog. 2008, 47:806-813.
58. Csibi A., Cornille K., Leibovitch M.P., Poupon A., Tintignac L.A., Sanchez A.M., Leibovitch S.A. The translation regulatory subunit eIF3f controls the kinase-dependent mTOR signaling required for muscle differentiation and hypertrophy in mouse. PLoS ONE 2010, 5:e8994.
59. Moretti J., Chastagner P., Gastaldello S., Heuss S.F., Dirac A.M., Bernards R., Masucci M.G., Israel A., Brou C. The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation. PLoS Biol. 2010, 8:e1000545.
60. Burnicka-Turek O., Kata A., Buyandelger B., Ebermann L., Kramann N., Burfeind P., Hoyer-Fender S., Engel W., Adham I.M. Pelota interacts with HAX1, EIF3G and SRPX and the resulting protein complexes are associated with the actin cytoskeleton. BMC Cell Biol. 2010, 11:28.
61. Nupponen N.N., Isola J., Visakorpi T. Mapping the amplification of EIF3S3 in breast and prostate cancer. Genes Chromosom. Cancer 2000, 28:203-210.
62. Savinainen K.J., Linja M.J., Saramaki O.R., Tammela T.L., Chang G.T., Brinkmann A.O., Visakorpi T. Expression and copy number analysis of TRPS1, EIF3S3 and MYC genes in breast and prostate cancer. Br. J. Cancer 2004, 90:1041-1046.
63. Nupponen N.N., Porkka K., Kakkola L., Tanner M., Persson K., Borg A., Isola J., Visakorpi T. Amplification and overexpression of p40 subunit of eukaryotic translation initiation factor 3 in breast and prostate cancer. Am. J. Pathol. 1999, 154:1777-1783.
64. Saramaki O., Visakorpi T. Chromosomal aberrations in prostate cancer. Front. Biosci.: J. Virt. Libr. 2007, 12:3287-3301.
65. Okamoto H., Yasui K., Zhao C., Arii S., Inazawa J. PTK2 and EIF3S3 genes may be amplification targets at 8q23-q24 and are associated with large hepatocellular carcinomas. Hepatology 2003, 38:1242-1249.
66. Cappuzzo F., Varella-Garcia M., Rossi E., Gajapathy S., Valente M., Drabkin H., Gemmill R. MYC and EIF3H Coamplification significantly improve response and survival of non-small cell lung cancer patients (NSCLC) treated with gefitinib. J. Thorac. Oncol.: Off. Pub. Int. Assoc. Study Lung Can. 2009, 4:472-478.
67. Chen R.H., Miettinen P.J., Maruoka E.M., Choy L., Derynck R. A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor. Nature 1995, 377:548-552.
68. Joseph P., Lei Y.X., Ong T.M. Up-regulation of expression of translation factors - a novel molecular mechanism for cadmium carcinogenesis. Mol. Cell. Biochem. 2004, 255:93-101.
69. Huang J.S., Chao C.C., Su T.L., Yeh S.H., Chen D.S., Chen C.T., Chen P.J., Jou Y.S. Diverse cellular transformation capability of overexpressed genes in human hepatocellular carcinoma. Biochem. Biophys. Res. Commun. 2004, 315:950-958.
70. Choy L., Derynck R. The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts as a modulator of the TGF-beta response. J. Biol. Chem. 1998, 273:31455-31462.
71. Bierie B., Moses H.L. Transforming growth factor beta (TGF-beta) and inflammation in cancer. Cytokine Growth Factor Rev. 2010, 21:49-59.
72. Blobe G.C., Schiemann W.P., Lodish H.F. Role of transforming growth factor beta in human disease. New Engl. J. Med. 2000, 342:1350-1358.
73. Fraser H.B., Hirsh A.E., Giaever G., Kumm J., Eisen M.B. Noise minimization in eukaryotic gene expression. PLoS Biol. 2004, 2:e137.
74. Fraser C.S. Chapter 1 the molecular basis of translational control. Prog. Mol. Biol. Transl. Sci. 2009, 90:1-51.
75. Unbehaun A., Borukhov S.I., Hellen C.U., Pestova T.V. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev. 2004, 18:3078-3093.
76. Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W. Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3. Eur. J. Biochem./FEBS 2003, 270:4133-4139.
77. Wei Z., Zhang P., Zhou Z., Cheng Z., Wan M., Gong W. Crystal structure of human eIF3k, the first structure of eIF3 subunits. J. Biol. Chem. 2004, 279:34983-34990.
78. Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J. Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k) as a new interaction partner of cyclin D3. FEBS Lett. 2004, 573:139-146.
79. Lin Y.M., Chen Y.R., Lin J.R., Wang W.J., Inoko A., Inagaki M., Wu Y.C., Chen R.H. EIF3k regulates apoptosis in epithelial cells by releasing caspase 3 from keratin-containing inclusions. J. Cell Sci. 2008, 121:2382-2393.
80. Goh S.H., Hong S.H., Lee B.C., Ju M.H., Jeong J.S., Cho Y.R., Kim I.H., Lee Y.S. eIF3m expression influences the regulation of tumorigenesis-related genes in human colon cancer. Oncogene 2011, 30:398-409.
81. Gingras A.C., Raught B., Sonenberg N. EIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 1999, 68:913-963.
82. 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, 12:1234-1238.
83. Nielsen K.H., Behrens M.A., He Y., Oliveira C.L., Sottrup Jensen L., Hoffmann S.V., Pedersen J.S., Andersen G.R. Synergistic activation of eIF4A by eIF4B and eIF4G. Nucleic Acids Res. 2011, 39:2678-2689.
84. Shahbazian D., Parsyan A., Petroulakis E., Hershey J., Sonenberg N. eIF4B controls survival and proliferation and is regulated by proto-oncogenic signaling pathways. Cell Cycle 2010, 9:4106-4109.
85. Kroczynska B., Kaur S., Katsoulidis E., Majchrzak-Kita B., Sassano A., Kozma S.C., Fish E.N., Platanias L.C. Interferon-dependent engagement of eukaryotic initiation factor 4B via S6 kinase (S6K)- and ribosomal protein S6K-mediated signals. Mol. Cell. Biol. 2009, 29:2865-2875.
86. Noske A., Lindenberg J.L., Darb-Esfahani S., Weichert W., Buckendahl A.C., Roske A., Sehouli J., Dietel M., Denkert C. Activation of mTOR in a subgroup of ovarian carcinomas: correlation with p-eIF-4E and prognosis. Oncol. Rep. 2008, 20:1409-1417.
87. Fukuchi-Shimogori T., Ishii I., Kashiwagi K., Mashiba H., Ekimoto H., Igarashi K. Malignant transformation by overproduction of translation initiation factor eIF4G. Cancer Res. 1997, 57:5041-5044.
88. Chen G.G., Lai P.B., Ho R.L., Chan P.K., Xu H., Wong J., Lau W.Y. Reduction of double-stranded RNA-activated protein kinase in hepatocellular carcinoma associated with hepatitis B virus. J. Med. Virol. 2004, 73:187-194.
89. Peffley D.M., Sharma C., Hentosh P., Buechler R.D. Perillyl alcohol and genistein differentially regulate PKB/Akt and 4E-BP1 phosphorylation as well as eIF4E/eIF4G interactions in human tumor cells. Arch. Biochem. Biophys. 2007, 465:266-273.
90. Li B.D., Liu L., Dawson M., De Benedetti A. Overexpression of eukaryotic initiation factor 4E (eIF4E) in breast carcinoma. Cancer 1997, 79:2385-2390.
91. Rosenwald I.B., Chen J.J., Wang S., Savas L., London I.M., Pullman J. Upregulation of protein synthesis initiation factor eIF-4E is an early event during colon carcinogenesis. Oncogene 1999, 18:2507-2517.
92. Sorrells D.L., Ghali G.E., De Benedetti A., Nathan C.O., Li B.D. Progressive amplification and overexpression of the eukaryotic initiation factor 4E gene in different zones of head and neck cancers. J. Oral Max. Surg: Off. J. Am. Assoc. Oral Maxill. Surg. 1999, 57:294-299.
93. Kevil C.G., De Benedetti A., Payne D.K., Coe L.L., Laroux F.S., Alexander J.S. Translational regulation of vascular permeability factor by eukaryotic initiation factor 4E: implications for tumor angiogenesis. Int. J. Can. J. Int. du Can. 1996, 65:785-790.
94. Lazaris-Karatzas A., Smith M.R., Frederickson R.M., Jaramillo M.L., Liu Y.L., Kung H.F., Sonenberg N. Ras mediates translation initiation factor 4E-induced malignant transformation. Genes Dev. 1992, 6:1631-1642.
95. Tu L., Liu Z., He X., He Y., Yang H., Jiang Q., Xie S., Xiao G., Li X., Yao K., Fang W. Over-expression of eukaryotic translation initiation factor 4 gamma 1 correlates with tumor progression and poor prognosis in nasopharyngeal carcinoma. Mol. Can. 2010, 9:78.
96. Brass N., Ukena I., Remberger K., Mack U., Sybrecht G.W., Meese E.U. DNA amplification on chromosome 3q26.1-q26.3 in squamous cell carcinoma of the lung detected by reverse chromosome painting. Eur. J. Cancer 1996, 32A:1205-1208.
97. Comtesse N., Keller A., Diesinger I., Bauer C., Kayser K., Huwer H., Lenhof H.P., Meese E. Frequent overexpression of the genes FXR1, CLAPM1 and EIF4G located on amplicon 3q26-27 in squamous cell carcinoma of the lung. Int. J. Can. J. Int. du Can. 2007, 120:2538-2544.
98. Riazimand S.H., Welkoborsky H.J., Bernauer H.S., Jacob R., Mann W.J. Investigations for fine mapping of amplifications in chromosome 3q26.3-28 frequently occurring in squamous cell carcinomas of the head and neck. Oncology 2002, 63:385-392.
99. Rao P.H., Arias-Pulido H., Lu X.Y., Harris C.P., Vargas H., Zhang F.F., Narayan G., Schneider A., Terry M.B., Murty V.V. Chromosomal amplifications, 3q gain and deletions of 2q33-q37 are the frequent genetic changes in cervical carcinoma. BMC Can. 2004, 4:5.
100. Sattler H.P., Lensch R., Rohde V., Zimmer E., Meese E., Bonkhoff H., Retz M., Zwergel T., Bex A., Stoeckle M., Wullich B. Novel amplification unit at chromosome 3q25-q27 in human prostate cancer. Prostate 2000, 45:207-215.
101. Conte M.R., Kelly G., Babon J., Sanfelice D., Youell J., Smerdon S.J., Proud C.G. Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry 2006, 45:4550-4558.
102. Jennings M.D., Pavitt G.D. eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation. Nature 2010, 465:378-381.
103. Bieniossek C., Schutz P., Bumann M., Limacher A., Uson I., Baumann U. The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J. Mol. Biol. 2006, 360:457-465.
104. Singh C.R., Lee B., Udagawa T., Mohammad-Qureshi S.S., Yamamoto Y., Pavitt G.D., Asano K. An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. Nature 2010, 465:378-381.
105. Maag D., Algire M.A., Lorsch J.R. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. J. Mol. Biol. 2006, 356:724-737.
106. Sheu J.J., Lee C.H., Ko J.Y., Tsao G.S., Wu C.C., Fang C.Y., Tsai F.J., Hua C.H., Chen C.L., Chen J.Y. Chromosome 3p12.3-p14.2 and 3q26.2-q26.32 are genomic markers for prognosis of advanced nasopharyngeal carcinoma. Can. Epidemiol., Biomarkers & Prevent.: a Pub. Am. Assoc. Can. Res., Cosponsored Am. Soc. Prev. Oncol. 2009, 18:2709-2716.
107. Houlston R.S., Cheadle J., Dobbins S.E., Tenesa A., Jones A.M., Howarth K., Spain S.L., Broderick P., Domingo E., Farrington S., Prendergast J.G., Pittman A.M, Theodoratou E., Smith C.G., Olver B., Walther A., Barnetson R.A., Churchman M., Jaeger E.E., Penegar S., Barclay E., Martin L., Gorman M., Mager R., Johnstone E., Midgley R., Niittymaki I., Tuupanen S., Colley J., Idziaszczyk S., Thomas H.J., Lucassen A.M., Evans D.G., Maher E.R., Maughan T., Dimas A., Dermitzakis E., Cazier J.B., Aaltonen L.A., Pharoah P., Kerr D.J, Carvajal-Carmona L.G., Campbell H., Dunlop M.G., Tomlinson I.P. Meta-analysis of three genome-wide association studies identifies susceptibility loci for colorectal cancer at 1q41, 3q26.2, 12q13.13 and 20q13.33. Nat Genet. 2010, 42:973-977.
108. Policht F.A., Song M., Sitailo S., O'Hare A., Ashfaq R., Muller C.Y., Morrison L.E., King W., Sokolova I.A. Analysis of genetic copy number changes in cervical disease progression. BMC Can. 2010, 10:432.
109. Hussenet T., Dali S., Exinger J., Monga B., Jost B., Dembele D., Martinet N., Thibault C., Huelsken J., Brambilla E., du Manoir S. SOX2 is an oncogene activated by recurrent 3q26.3 amplifications in human lung squamous cell carcinomas. PLoS One 2010, 5:e8960.
110. Yang G.F., Xie D., Liu J.H., Luo J.H., Li L.J., Hua W.F., Wu H.M., Kung H.F., Zeng Y.X., Guan X.Y. Expression and amplification of eIF-5A2 in human epithelial ovarian tumors and overexpression of EIF-5A2 is a new independent predictor of outcome in patients with ovarian carcinoma. Gynecol. Oncol. 2009, 112:314-318.
111. Maier B., Ogihara T., Trace A.P., Tersey S.A., Robbins R.D., Chakrabarti S.K., Nunemaker C.S., Stull N.D., Taylor C.A., Thompson J.E., Dondero R.S., Lewis E.C., Dinarello C.A., Nadler J.L., Mirmira R.G. The unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice. J. Clin. Invest. 2010, 120:2156-2170.
112. Balabanov S., Gontarewicz A., Ziegler P., Hartmann U., Kammer W., Copland M., Brassat U., Priemer M., Hauber I., Wilhelm T., Schwarz G., Kanz L., Bokemeyer C., Hauber J., Holyoake T.L., Nordheim A., Brummendorf T.H. Hypusination of eukaryotic initiation factor 5A (eIF5A): a novel therapeutic target in BCR-ABL-positive leukemias identified by a proteomics approach. Blood 2007, 109:1701-1711.
113. Miluzio A., Beugnet A., Volta V., Biffo S. Eukaryotic initiation factor 6 mediates a continuum between 60S ribosome biogenesis and translation. EMBO Rep. 2009, 10:459-465.
114. Benelli D., Marzi S., Mancone C., Alonzi T., la Teana A., Londei P. Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya. Nucleic Acids Res. 2009, 37:256-267.
115. Gandin V., Miluzio A., Barbieri A.M., Beugnet A., Kiyokawa H., Marchisio P.C., Biffo S. Eukaryotic initiation factor 6 is rate-limiting in translation, growth and transformation. Nature 2008, 455:684-688.
116. Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I., Liebhaber S.A., Pasquinelli A.E., Shiekhattar R. MicroRNA silencing through RISC recruitment of eIF6. Nature 2007, 447:823-828.
117. Sanvito F., Vivoli F., Gambini S., Santambrogio G., Catena M., Viale E., Veglia F., Donadini A., Biffo S., Marchisio P.C. Expression of a highly conserved protein, p27BBP, during the progression of human colorectal cancer. Cancer Res. 2000, 60:510-516.
118. Flavin R.J., Smyth P.C., Finn S.P., Laios A., O'Toole S.A., Barrett C., Ring M., Denning K.M., Li J., Aherne S.T., Aziz N.A., Alhadi A., Sheppard B.L., Loda M., Martin C., Sheils O.M., O'Leary J.J. Altered eIF6 and Dicer expression is associated with clinicopathological features in ovarian serous carcinoma patients. Mod. Path.: Off. J. United States Canadian Acad. Pathol., Inc 2008, 21:676-684.
119. Harris M.N., Ozpolat B., Abdi F., Gu S., Legler A., Mawuenyega K.G., Tirado-Gomez M., Lopez-Berestein G., Chen X. Comparative proteomic analysis of all-trans-retinoic acid treatment reveals systematic posttranscriptional control mechanisms in acute promyelocytic leukemia. Blood 2004, 104:1314-1323.
120. Rosso P., Cortesina G., Sanvito F., Donadini A., Di Benedetto B., Biffo S., Marchisio P.C. Overexpression of p27BBP in head and neck carcinomas and their lymph node metastases. Head Neck 2004, 26:408-417.
121. Wilkins J.A., Sansom O.J. C-Myc is a critical mediator of the phenotypes of Apc loss in the intestine. Cancer Res. 2008, 68:4963-4966.
122. Homma M.K., Wada I., Suzuki T., Yamaki J., Krebs E.G., Homma Y. CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cycle progression. Proc. Nat. Acad. Sci. USA 2005, 102:15688-15693.
123. Nanda J.S., Cheung Y.N., Takacs J.E., Martin-Marcos P., Saini A.K., Hinnebusch A.G., Lorsch J.R. EIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J. Mol. Biol. 2009, 394:268-285.
124. Saini A.K., Nanda J.S., Lorsch J.R., Hinnebusch A.G. Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNA(i)(Met) binding to the ribosome. Genes Dev. 2010, 24:97-110.
125. Yu Y., Marintchev A., Kolupaeva V.G., Unbehaun A., Veryasova T., Lai S.C., Hong P., Wagner G., Hellen C.U., Pestova T.V. Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing. Nucleic Acids Res. 2009, 37:5167-5182.
126. Mohammad-Qureshi S.S., Haddad R., Hemingway E.J., Richardson J.P., Pavitt G.D. Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange. Mol. Cell. Biol. 2007, 27:5225-5234.
127. Jiang H.Y., Jiang L., Wek R.C. The eukaryotic initiation factor-2 kinase pathway facilitates differential GADD45a expression in response to environmental stress. J. Biol. Chem. 2007, 282:3755-3765.
128. Horzinski L., Huyghe A., Cardoso M.C., Gonthier C., Ouchchane L., Schiffmann R., Blanc P., Boespflug-Tanguy O., Fogli A. Eukaryotic initiation factor 2B (eIF2B) GEF activity as a diagnostic tool for EIF2B-related disorders. PLoS ONE 2009, 4:e8318.
129. Wang X., Proud C.G. A novel mechanism for the control of translation initiation by amino acids, mediated by phosphorylation of eukaryotic initiation factor 2B. Mol. Cell. Biol. 2008, 28:1429-1442.
130. Sha Z., Brill L.M., Cabrera R., Kleifeld O., Scheliga J.S., Glickman M.H., Chang E.C., Wolf D.A. The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries. Mol. Cell 2009, 36:141-152.
131. Marintchev A., Edmonds K.A., Marintcheva B., Hendrickson E., Oberer M., Suzuki C., Herdy B., Sonenberg N., Wagner G. Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation. Cell 2009, 136:447-460.
132. 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. 2005, 79:8057-8064.
133. Cheng S., Sultana S., Goss D.J., Gallie D.R. Translation initiation factor 4B homodimerization, RNA binding, and interaction with Poly(A)-binding protein are enhanced by zinc. J. Biol. Chem. 2008, 283:36140-36153.
134. D.W. Martindale, M.D. Wilson, D. Wang, R.D. Burke, X. Chen, V. Duronio, B.F. Koop, Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23. Mamm. Genome: Off. J. Int. Mamm. Genome Soc. 11 (2000) 890-898.
135. Wu D., Matsushita K., Matsubara H., Nomura F., Tomonaga T. An alternative splicing isoform of eukaryotic initiation factor 4H promotes tumorigenesis in vivo and is a potential therapeutic target for human cancer. Int. J. Can. J. Int. du Can. 2011, 128:1018-1030.
136. Jennings M.D., Pavitt G.D. EIF5 has GDI activity necessary for translational control by eIF2 phosphorylation. Nature 2010, 465:378-381.
137. Tu L., Liu Z., He X., He Y., Yang H., Jiang Q., Xie S., Xiao G., Li X., Yao K., Fang W. Over-expression of eukaryotic translation initiation factor 4 gamma 1 correlates with tumor progression and poor prognosis in nasopharyngeal carcinoma. Mol. Can. 2010, 9:78.
138. Goh S.H., Hong S.H., Hong S.H., Lee B.C., Ju M.H., Jeong J.S., Cho Y.R., Kim I.H., Lee Y.S. EIF3m expression influences the regulation of tumorigenesis-related genes in human colon cancer. Oncogene 2011, 30:398-409.
139. Haybaeck J., O'Connor T., Spilka R., Spizzo G., Ensinger C., Mikuz G., Brunhuber T., Vogetseder A., Theurl I., Salvenmoser W., Draxl H., Banziger R., Bachmann F., Schafer G., Burger M., Obrist P. Overexpression of p150, a part of the large subunit of the eukaryotic translation initiation factor 3, in colon cancer. Anticancer Res. 2010, 30:1047-1055.
140. Maier B., Ogihara T., Trace A.P., Tersey S.A., Robbins R.D., Chakrabarti S.K., Nunemaker C.S., Stull N.D., Taylor C.A., Thompson J.E., Dondero R.S., Lewis E.C., Dinarello C.A., Nadler J.L., Mirmira R.G. The unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice. J. Clin. Investig. 2010, 120:2156-2170.
141. Pöyry T.A., Kaminski A., Jackson R.J. What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?. Genes Dev. 2004, 18:62-75.
142. Baird T.D., Wek R.C. Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism. Adv. Nutr. 2012, 3:307-321.
143. Liu Y., László C., Liu Y., Liu W., Chen X., Evans S.C., Wu S. Regulation of G1 arrest and apoptosis in hypoxia by PERK and GCN2-mediated eIF2alpha phosphorylation. Neoplasia 2010, 12:61-68.
144. Raught B., Gingrad A.C., James A., Medina D., Sonenberg N., Rosen J.M. Expression of a translationally regulated, dominant-negative CCAAT/enhancer-binding protein beta isoform and up-regulation of the eukaryotic translation initiation factor 2alpha are correlated with neoplastic transformation of mammary epithelial cells. Cancer Res. 1996, 56:4382-4386.
145. Gallagher J.W., Kubica N., Kimball S.R., Jefferson L.S. Reduced eukaryotic initiation factor 2B epsilon-subunit expression suppresses the transformed phenotype of cells overexpressing the protein. Cancer Res. 2008, 68:8752-8760.
146. Schewe D.M., Aquirre-Ghiso J.A. Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy. Cancer Res. 2009, 69:1545-1552.
147. Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W., Doudna J.A., Robinson C.V. Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3. PNAS 2008, 105:18139-18144.
148. C. Sun, A. Todorovic, J. Querol-Audi, Y. Bai, N. Villa, M. Snyder, J. Ashchyan, C.S. Lewis, A. Hartland, S. Gradia, C.F. Fraser, J.A. Doudna, E. Nogales, J.H.D. Cate, Functional reconstitiution of human eukaryotic translation initiation factor 3 (eIF3). PNAS (2011) 1116821108.
149. Sudo H., Tsuji A.B., Sugyo A., Kohda M., Sogawa C., Yoshida C., Harada Y., Hino O., Saga T. Kockdown of COPA, indentified by loss-of-function screen, induces apoptosis and supresses tumor growth in mesothelioma mouse model. Genomics 2010, 95:201-226.
150. Liu R.Y., Dong Z., Liu J., et al. Role of eIF3a in regulating cisplatin sensitivity and in translational control of nucleotide excision repair of nasopharyngeal carcinoma. Oncogene 2011, 30:4814-4823.
151. Yin J.Y., Shen J., Dong Z.Z., et al. Effect of eIF3a on response of lung cancer patients to platinum-based chemotherapy by regulating DNA repair. Clin. Cancer Res. 2011, 17:4600-4609.
152. R. Spilka, K. Laimer, F. Bachmann, G. Spizzo, A. Vogetseder, M. Wieser, H. Müller, J. Haybaeck, P. Obrist, Overexpression of eIF3a in squamous cell carcinoma of the oral cavity and its putative relation to chemotherapy response. J. Oncol. (2012) 901956.
153. Lagirand-Cantaloube J., Offner N., Csibi A., Leibovitch M.P., Batonnet-Pichon S., Tintignac L.A., Segura C.T., Leibovitch S.A. The initiation factor eIF3f is a major target for Atrogin1/MAFbx function in skeletal muscle atrophy. EMBO J. 2008, 27:1266-1276.
154. Cheshenko N., Trepanier J.B., Segarra T.J., Fuller A.O., Herold B.C. HSV usurps eukaryotic initiation factor 3 subunit M for viral protein translation: novel prevention target. PLoS ONE 2010, 5:e11829.
155. Malina A., Cencic R., Pelletier J. Targeting translation dependence in cancer. Oncotarget 2011, 2:76-88.
156. Jia Y., Chiu T.L., Amin E.A., Polunovsky V., Bitterman P.B., Wagner C.R. Design, synthesis and evaluation of analogs of initiation factor 4E (eIF4E) cap-binding antagonist Bn7-GMP. Eur. J. Med. Chem. 2010, 45:1304-1313.
157. Grzmil M., Hemmings B.A. Translation regulation as a therapeutic target in cancer. Cancer Res. 2012, 72:3891-3900.
158. J.Y. Yin, Z. Dong, Z.Q. Liu, J.T. Zhang, Translational control gone awry: a new mechanism of tumorigenesis and novel targets of cancer treatments. Biosci. Rep. 31 (2011).
159. Hagner P.R., Schneider A., Gartenhaus R.B. Targeting the translational machinery as a novel treatment strategy for hematologic malignancies 2010, Blood, 115:2127-2135.
160. Lindqvist L., Pelletier J. Inhibitors of translation initiation as cancer therapeutics. Future Med. Chem. 2009, 1:1709-1722.
161. Robert F., Pelletier J. Translation initiation: a critical signalling node in cancer. Expert Opin. Ther. Targets 2009, 13:1279-1293.
162. Graff J.R., Konicek B.W., Carter J.H., Marcusson E.G. Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res. 2008, 68:631-634.
163. Alain T., Morita M., Fonseca B.D., Yanagiya A., Siddiqui N., Bhat M., Zammit D., Marcus V., Metrakos P., Voyer L.A., Gandin V., Liu Y., Topisirovic I., Sonenberg N. EIF4E/4E-BP ratio predicts the efficacy of mTOR targeted therapies. Cancer Res. 2012, 72:6468-6476.
164. Assouline S., Culjkovic B., Cocolakis E., Rousseau C., Beslu N., Amri A., Caplan S., Leber B., Roy D.C., Miller W.H., Borden K.L. Molecular targeting of the oncogene eIF4E in acute myeloid leukemia (AML): a proof-of-principle clinical trial with ribavirin. Blood 2009, 114:257-260.
165. Nasr Z., Robert F., Porco J.A., Muller W.J., Pelletier J. EIF4F suppression in breast cancer affects maintenance and progression. Oncogene 2013, 32:861-871.
166. L. Chen, B.H. Aktas, Y. Wang, X. He, R. Sahoo, N. Zhang, S. Denoyelle, E. Kabha, H. Yang, R.Y. Freedman, J.G. Supko, M. Chorev, G. Wagner, J.A. Halperin, Tumor suppression by small molecule inhibitors of translation initiation. Oncotarget 3 (2012) 869-81.