Abstract
The v-myc oncogene was first identified in 1977 as the transforming gene of the MC29 avian retrovirus, which causes myelocytomatosis, carcinomas, and sarcomas in chickens [1]. The c-myc proto-oncogene has since been identified in a wide variety of organisms ranging from the invertebrate sea star [2] to humans [3]. Deregulated expression of a normal c-myc gene leads to malignant transformation in certain cell culture models, such as primary rat embryo fibroblasts (REF; in which the coexpression of a second activated oncogene, ras, is also required) [4,5], and in transgenic mice [6] and rabbits [7]. Burkitt lymphoma, a naturally occurring human tumor, provides a paradigm for the role of c-myc in malignant transformation. In this case, chromosomal translocation of the c-myc locus to a location downstream of the regulatory elements of the immunoglobulin heavy chain gene results in deregulated expression of c-myc [8]. In contrast to many other oncogenes that have activating mutations in the coding sequence, this deregulated expression of a normal c-myc coding sequence appears to be responsible for the oncogenic contribution of c-myc [4].
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References
Duesberg PH, Bister K, Vogt PK: The RNA of avian acute leukemia virus MC29, Proc Natl Acad Sci USA 74:4320–4324, 1977.
Walker CW, Boom JDG, Marsh AG: First non-vertebrate member of the c-myc family is seasonally expressed in an invertebrate testis. Oncogene, in press, 1992.
Dalla Favera R, Bregni M, Erikson J, Patterson D, Gallo RC, Croce CM: Human c-myc oncogene is located on the region of chromosome 8 that is translocated in Burkitt lymphoma cells. Proc Natl Acad Sci USA 79:7824–7827, 1982.
Lee WM, Schwab M, Westaway D, Varmus HE: Augmented expression of normal c-myc is sufficient for cotransformation of rat embryo cells with a mutant ras gene. Mol Cell Biol 5:3345–3356, 1985.
Land H, Parada LF, Weinberg RA: Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes. Nature 304:596–602, 1983.
Adams JM, Harris AW, Pinkert CA, Corcoran LM, Alexander WS, Cory S, Palmiter RD, Brinster RL: The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice. Nature 318:533–538, 1985.
Knight KL, Spiker-Polet H, Kazdin DS, Oi VT: Transgenic rabbits with lymphocytic leukemia induced by the c-myc oncogene fused with the immunoglobulin heavy chain enhancer. Proc Natl Acad Sci USA 85:3130–3134, 1988.
Taub R, Kirsch I, Morton C, Lenoir G, Swan D, Tronick S, Aaronson S, Leder P: Translocation of the c-myc gene into the immunoglobulin heavy chain locus in human Burkitt lymphoma and murine plasmacytoma cells. Proc Natl Acad Sci USA 79:7837–7841, 1982.
DePinho RA, Schreiber-Agus N, Alt FW: myc family oncogenes in the development of normal and neoplastic cells. Adv Cancer Res 57:1–46, 1991.
Hann SR, King MW, Bentley DL, Anderson CW, Eisenman RN: A non-AUG translational initiation in c-myc exon 1 generates an N-terminally distinct protein whose synthesis is disrupted in Burkitt’s lymphomas. Cell 52:185–195, 1988.
Collum RG, Alt FW: Are Myc proteins transcription factors? Cancer Cells 2:69–75, 1990.
Luscher B, Eisenman RN: New light on Myc and Myb. Part 1. Myc. Genes Dev 4:2025–2035, 1990.
Murre C, McCaw PS, Baltimore D: A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and Myc proteins. Cell 56:777–783, 1989.
Prendergast GC, Ziff EB: Methylation-sensitive sequence-specific DNA binding by the c-Myc basic region. Science 251:186–189, 1991.
Blackwell TK, Kretzner L, Blackwood EM, Eisenman RN, Weintraub H: Sequence-specific DNA binding by the c-Myc protein. Science 250:1149–1151, 1990.
Stone J, de Lange T, Ramsay G, Jakobovits E, Bishop JM, Varmus H, Lee W: Definition of regions in human c-Myc that are involved in transformation and nuclear localization. Mol Cell Biol 7:1697–1709, 1987.
Schwab M, Alitalo K, Klempnauer KH, Varmus HE, Bishop JM, Gilbert F, Brodeur G, Goldstein M, Trent J: Amplified DNA with limited homology to myc cellular oncogene is shared by human neuroblastoma cell lines and a neuroblastoma tumour. Nature 305:245–248, 1983.
Kohl NE, Kanda N, Schreck RR, Bruns G, Latt SA, Gilbert F, Alt FW: Transposition and amplification of oncogene-related sequences in human neuroblastomas. Cell 35:359–367, 1983.
Nau MM, Brooks BJ, Battey J, Sausville E, Gazdar AF, Kirsch IR, McBride OW, Bertness V, Hollis GF, Minna JD: L-myc, a new myc-related gene amplified and expressed in human small cell lung cancer. Nature 318:69–73, 1985.
Blackwood EM, Eisenman RN: Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251:1211–1217, 1991.
Suzuki M: SPXX, a frequent sequence motif in gene regulatory proteins. J Mol Biol 207:61–84, 1989.
Dang CV, van Dam H, Buckmire M, Lee WM: DNA-binding domain of human c-Myc produced in Escherichia coli. Mol Cell Biol 9:2477–2486, 1989.
Kato GJ, Dang CV: Function of the c-Myc oncoprotein. FASEB J 6:3065–3072, 1992.
Sarid J, Halazonetis TD, Murphy W, Leder P: Evolutionarily conserved regions of the human c-Myc protein can be uncoupled from transforming activity. Proc Natl Acad Sci USA 84:170–173, 1987.
Kato GJ, Barrett J, Villa Garcia M, Dang CV: An amino-terminal c-Myc domain required for neoplastic transformation activates transcription. Mol Cell Biol 10:5914–5920, 1990.
Dang CV, Lee WM: Identification of the human c-Myc protein nuclear translocation signal. Mol Cell Biol 8:4048–4054, 1988.
Murre C, McCaw PS, Vaessin H, Caudy M, Jan LY, Jan YN, Cabrera CV, Buskin JN, Hauschka SD, Lassar AB: Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence. Cell 58:537–544, 1989.
Clarke MF, Kukowska Latallo JF, Westin E, Smith M, Prochownik EV: Constitutive expression of a c-myb cDNA blocks Friend murine erythroleukemia cell differentiation. Mol Cell Biol 8:884–892, 1988.
Anthony-Cahil SJ, Benfield PA, Fairman R, Wasserman ZR, Brenner SL, Stafford III WF, Altenbach C, Hubbell WL, DeGrado WF: Molecular characterization of helix-loop-helix peptides. Science 255:979–983, 1992.
Voronova A, Baltimore D: Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains. Proc Natl Acad Sci USA 87:4722–4726, 1990.
Beckman H, Su LK, Kadesch T: TFE3: A helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif. Genes Dev 4:167–179, 1990.
Gregor PD, Sawadogo M, Roeder RG: The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer. Genes Dev 4:1730–1740, 1990.
Hu YF, Luscher B, Admon A, Mermod N, Tjian R: Transcription factor AP-4 contains multiple dimerization domains that regulate dimer specificity. Genes Dev 4:1741–1752, 1990.
Landschulz WH, Johnson PF, McKnight SL: The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins. Science 240:1759–1764, 1988.
Beckmann H, Kadesch T: The leucine zipper of TFE3 dictates helix-loop-helix dimerization specificity. Genes Dev 5:1057–1066, 1991.
Kato GJ, Lee WM, Chen LL, Dang CV: Max: Functional domains and interaction with c-Myc. Genes Dev 6:81–92, 1992.
Dang CV, Barrett J, Villa Garcia M, Resar LM, Kato GJ, Fearon ER: Intracellular leucine zipper interactions suggest c-Myc hetero-oligomerization. Mol Cell Biol 11:954–962, 1991.
Prendergast GC, Lawe D, Ziff EB: Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation-sensitive DNA binding and ras cotransformation. Cell 65:395–407, 1991.
Wenzel A, Czielpluch C, Hamann U, Schurmann J, Schwab M: The N-Myc oncoprotein is associated in vivo with the phosphoprotein Max (p20/22) in human neuroblastoma cells. EMBO J 10:3703–3712, 1991.
Dang CV, Dolde C, Gillison ML, Kato GJ: Discrimination between related DNA sites by a single amino acid residue of Myc-related basic-helix-loop-helix proteins. Proc Natl Acad Sci USA 89:599–602, 1992.
Cai M, Davis RW: Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy. Cell 61:437–446, 1990.
Halazonetis TD, Kandil AN: Determination of the c-MYC DNA-binding site. Proc Natl Acad Sci USA 88:6162–6166, 1991.
Papoulas O, Williams NG, Kingston RE: DNA-binding activities of c-Myc purified from eukaryotic cells. J Biol Chem, in press, 1992.
Eilers M, Schirm S, Bishop JM: The MYC protein activates transcription of the alpha-prothymosin gene. EMBO J 10:133–141, 1991.
Dang CV, McGuire M, Buckmire M, Lee WM: Involvement of the ‘leucine zipper’ region in the oligomerization and transforming activity of human c-Myc protein. Nature 337:664–666, 1989.
Sawyers CL, Callahan W, Witte ON: Dominant negative myc blocks transformation by ABL oncogenes. Cell 70:901–910, 1992.
Mitchell PJ, Tjian R: Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins. Science 245:371–378, 1989.
Mermelstein FH, Flores O, Reinberg D: Initiation of transcription by RNA polymerase II. Biochim Biophys Acta 1009:1–10, 1989.
Kerppola TK, Curran T: Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity. Cell 66:317–326, 1991.
Gartenberg MR, Crothers DM: Synthetic DNA bending sequences increase the rate of in vitro transcription initiation at the Escherichia coli lac promoter. J Mol Biol 219:217–230, 1991.
Zinkel SS, Crothers DM: Catabolite activator protein-induced DNA bending in transcription initiation. J Mol Biol 219:201–215, 1991.
Wechsler DS, Dang CV: Opposite orientations of DNA bending by c-Myc and Max. Proc Natl Acad Sci USA 89:7635–7639, 1992.
Suzuki M: SPKK, a new nucleic acid-binding unit of protein found in histone. EMBO J 8:797–804, 1989.
von Hippel PH, Berg OG: Facilitated target location in biological systems. J Biol Chem 264:675–678, 1989.
Luscher B, Kuenzel EA, Krebs EG, Eisenman RN: A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression. EMBO J 8:1111–1119, 1989.
Berberich SJ, Cole MD: Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers. Genes Dev 6:166–176, 1992.
Cole MD: Myc meets its Max. Cell 65:715–716, 1991.
Blackwood EM, Luscher B, Eisenman RN: Myc and Max associate in vivo. Genes Dev 6:71–80, 1992.
Amati B, Dalton S, Brooks MW, Littlewood TD, Evan GI, Land H: Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max. Nature 359:423–426, 1992.
Kretzner L, Blackwood EM, Eisenman RN: Myc and Max proteins possess distinct transcriptional activities. Nature 359:426–429, 1992.
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Kato, G.J., Wechsler, D.S., Dang, C.V. (1993). DNA binding by the Myc oncoproteins. In: Benz, C.C., Liu, E.T. (eds) Oncogenes and Tumor Suppressor Genes in Human Malignancies. Cancer Treatment and Research, vol 63. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3088-6_16
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DOI: https://doi.org/10.1007/978-1-4615-3088-6_16
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