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Research Article

Function of the c-Myc Antagonist Mad1 during a Molecular Switch from Proliferation to Differentiation

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Pages 2353-2359 | Received 20 Nov 1996, Accepted 28 Jan 1997, Published online: 29 Mar 2023

REFERENCES

  • Amati, B., M. W. Brooks, N. Levy, T. D. Littlewood, G. I. Evan, and H. Land. 1993. Oncogenic activity of the c-Myc protein requires dimerization with Max. Cell 72:233–245.
  • Amati, B., S. Dalton, M. W. Brooks, T. D. Littlewood, G. I. Evan, and H. Land. 1992. Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max. Nature 359:423–426.
  • Amin, C., A. J. Wagner, and N. Hay. 1993. Sequence-specific transcriptional activation by Myc and repression by Max. Mol. Cell. Biol. 13:383–390.
  • Ayer, D. E., and R. N. Eisenman. 1993. A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. Genes Dev. 7:2110–2119.
  • Ayer, D. E., L. Kretzner, and R. N. Eisenman. 1993. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72:211–222.
  • Ayer, D. E., C. D. Laherty, Q. A. Lawrence, A. P. Armstrong, and R. N. Eisenman. 1996. Mad proteins contain a dominant transcription repression domain. Mol. Cell. Biol. 16:5772–5781.
  • Ayer, D. E., Q. A. Lawrence, and R. N. Eisenman. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80:767–776.
  • Bar-Ner, M., L. T. Messing, C. M. Cultraro, M. J. Birrer, and S. Segal. 1992. Regions within the c-Myc protein that are necessary for transformation are also required for inhibition of differentiation of murine erythroleukemia cells. Cell Growth Differ. 3:183–190.
  • Bello-Fernandez, C., G. Packham, and J. L. Clevland. 1993. The ornithine decarboxylase gene is a transcriptional target of c-Myc. Proc. Natl. Acad. Sci. USA 90:7804–7808.
  • Blackwood, E. M., and R. N. Eisenman. 1991. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251:1211–1217.
  • Blackwood, E. M., B. Luscher, and R. N. Eisenman. 1992. Myc and Max associate in vivo. Genes Dev. 6:71–80.
  • Cerni, C., K. Bousset, C. Seelos, H. Burkhardt, M. Henriksson, and B. Luscher. 1995. Differential effects by Mad and Max on transformation by cellular and viral oncoproteins. Oncogene 11:587–596.
  • Chen, J., T. Willingham, L. R. Margraf, N. Schreiber-Agus, R. A. DePinho, and P. D. Nisen. 1995. Effects of the MYC oncogene antagonist, MAD, on proliferation, cell cycling and the malignant phenotype of human brain tumor cells. Nat. Med. 1:638–643.
  • Chin, L., N. Schreiber-Agus, I. Pellicer, K. Chen, H. Lee, M. Dudast, C. Cordon-Cardo, and R. A. DePinho. 1995. Contrasting roles for Myc and Mad proteins in cellular growth and differentiation. Proc. Natl. Acad. Sci. USA 92:8488–8492.
  • Cogliati, T., B. K. Dunn, M. Bar-Ner, C. M. Cultraro, and S. Segal. 1993. Transfected wild-type and mutant max regulate cell growth and differentiation of murine erythroleukemia cells. Oncogene 8:1263–1268.
  • Coppola, J. A., and M. D. Cole. 1986. Constitutive c-myc oncogene expression blocks mouse erythroleukaemia cell differentiation but not commitment. Nature 320:760–763.
  • Cowell, I. G. 1994. Repression versus activation in the control of gene transcription. Trends Biochem. Sci. 19:38–42.
  • Crouch, D. H., C. Lang, and D. A. F. Gillespie. 1990. The leucine zipper domain of avian c-Myc is required for transformation and autoregulation. Oncogene 5:683–689.
  • Cultraro, C. M., T. Cogliati, L. E. Hearing, and S. Segal. 1996. Basic mutant Max reverses a c-Myc block to differentiation. Oncol. Rep. 3:141–146.
  • Davis, L. G., M. D. Dibner, and J. F. Battey. 1986. Basic methods in molecular biology. Elsevier Science Publishing Co., New York, N.Y.
  • Delgado, M. D., A. Lerga, M. Canelles, M. T. Gomez-Casares, and J. Leon. 1995. Differential regulation of Max and role of c-Myc during erythroid and myelomonocytic differentiation of K562 cells. Oncogene 10:1659–1665.
  • Dmitrovsky, E., W. M. Kuehl, G. F. Hollis, I. R. Kirsch, T. P. Bender, and S. Segal. 1986. Expression of a transfected human c-myc oncogene inhibits differentiation of a mouse erythroleukaemia cell line. Nature 322:748–750.
  • Dube, S. K., G. Gaedicke, G. Kluge, N. Weimann, B. J. Melderis, H. Stein-heider, G. Crozier, H. Beckmann, and W. Ostertag. 1974. Hemoglobin-synthesizing mouse and human erythroleukemic cell lines as model systems for the study of differentiation and control of gene expression, p. 99–135. In W. Nakar, T. Ono, T. Suigimura, and H. Sugano (ed.), Differentiation and control of malignancy in tumor cells. University of Tokyo Press, Tokyo, Japan.
  • Dunn, B. K., T. Cogliati, C. M. Cultraro, M. Bar-Ner, and S. Segal. 1994. Regulation of murine Max (Myn) parallels the regulation of c-Myc in differentiating murine erythroleukemia cells. Cell Growth Differ. 5:847–854.
  • Edelhoff, S., D. E. Ayer, A. S. Zervos, E. Steingrimsson, N. A. Jenkins, N. G. Copeland, R. N. Eisenman, R. Brent, and C. M. Disteche. 1994. Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins: MAD to human chromosome 2 and mouse chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome 19. Oncogene 9:665–668.
  • Eilers, M., S. Schirm, and J. M. Bishop. 1991. The MYC protein activates transcription of the a-prothymosin gene. EMBO J. 10:133–141.
  • Einat, M., D. Resnitzky, and A. Kimchi. 1985. Close link between reduction of c-myc expression by interferon and G0/G1 arrest. Nature 313:597–600.
  • Freytag, S. O. 1988. Enforced expression of the c-myc oncogene inhibits cell differentiation by precluding entry into a distinct predifferentiation state in G0/G1. Mol. Cell. Biol. 8:1614–1624.
  • Gu, W., K. Cechova, V. Tassi, and R. Dalla-Favera. 1993. Opposite regulation of gene transcription and cell proliferation by c-Myc and Max. Proc. Natl. Acad. Sci. USA 90:2935–2939.
  • Harper, S. E., Y. Qiu, and P. Sharp. 1996. Sin3 corepressor function in Myc-induced transcription and transformation. Proc. Natl. Acad. Sci. USA 93:8536–8540.
  • Henriksson, M., and G. Luscher. 1996. Proteins of the Myc network: essential regulators of cell growth and differentiation. Cancer Res. 68:110–182.
  • Hurlin, P. J., K. P. Foley, D. E. Ayer, R. N. Eisenman, D. Hanahan, and J. M. Arbeit. 1995. Regulation of Myc and Mad during epidermal differentiation and HPV-associated tumorigenesis. Oncogene 11:2487–2501.
  • Hurlin, P. J., C. Queva, D. E. Ayer, N. G. Copeland, N. A. Jenkins, and R. N. Eisenman. 1995. Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. EMBO J. 14:5646–5659.
  • Kaczmarek, L., J. K. Hyland, R. Watt, M. Rosenberg, and R. Baserga. 1985. Microinjected c-myc as a competence factor. Science 228:1313–1315.
  • Kahn, S. M., W. Jiang, C. Borner, K. O’Driscoll, and I. B. Weinstein. 1990. Construction of defined deletion mutants by thermal cycled fusion: applications to protein kinase C. Tech. J. Methods Cell Mol. Biol. 2:27–30.
  • Kato, G., W. M. F. Lee, L. Chen, and C. V. Dang. 1992. Max: functional domains and interaction with c-Myc. Genes Dev. 6:81–92.
  • Kato, G. J., J. Barrett, M. Villa-Garcia, and C. V. Dang. 1990. An amino-terminal c-Myc domain required for neoplastic transformation activates transcription. Mol. Cell. Biol. 10:5914–5920.
  • Klinken, P. S., K. L. Holmes, H. C. Morse, and S. S. Thorgeirsson. 1988. Transcriptional and post-transcriptional regulation of c-myc and p53 during proliferation and differentiation of murine erythroleukemia cells treated with DFMO and DMSO. Exp. Cell Res. 178:185–198.
  • Koskinen, P. J., D. E. Ayer, and R. N. Eisenman. 1995. Repression of Myc-Ras cotransformation by Mad is mediated by multiple protein-protein interactions. Cell Growth Differ. 6:623–629.
  • Kretzner, L., E. M. Blackwood, and R. N. Eisenman. 1992. Myc and Max proteins possess distinct transcriptional activities. Nature 359:426–429.
  • Lachman, H. M., and A. I. Skoultchi. 1984. Expression of c-myc changes during differentiation of mouse erythroleukemia cells. Nature 310:592–594.
  • Lahoz, E. G., L. Xu, N. Schreiber-Agus, and R. A. DePinho. 1994. Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1. Proc. Natl. Acad. Sci. USA 91:5503–5507.
  • Larsson, L., M. Pettersson, F. Oberg, K. Nilsson, and B. Luscher. 1994. Expression of mad, mxi1, max and c-myc during induced differentiation of hematopoietic cells: opposite regulation of mad and c-myc. Oncogene 9:1247–1252.
  • Levine, M., and J. L. Manley. 1989. Transcriptional repression of eukaryotic promoters. Cell 59:405–408.
  • Littlewood, T. D., B. Amati, H. Land, and G. I. Evan. 1992. Max and c-Myc/Max DNA-binding activities in cell extracts. Oncogene 7:1783–1792.
  • Lymboussaki, A., A. Kaipainen, E. Hatva, I. Vastrik, L. Jeskanen, M. Jal-kanen, S. Werner, R. Stenback, and R. Alitalo. 1996. Expression of Mad, an antagonist of Myc oncoprotein function, in differentiating keratinocytes during tumorigenesis of the skin. Br. J. Cancer 73:1347–1355.
  • Marcu, K. B., S. A. Bossone, and A. J. Patel. 1992. myc function and regulation. Annu. Rev. Biochem. 61:809–860.
  • Marks, P. A., V. M. Richon, J. Kiyokawa, and R. A. Rifkind. 1994. Inducing differentiation of transformed cells with hybrid polar compounds: a cell cycle-dependent process. Proc. Natl. Acad. Sci. USA 91:10251–10254.
  • Mechti, N., M. Piechaczyk, J. Blanchard, L. Marty, A. Bonnieu, P. Jeanteur, and B. Lebleu. 1986. Transcriptional and posttranscriptional regulation of c-myc expression during differentiation of murine erythroleukemia Friend cells. Nucleic Acids Res. 14:9653–9666.
  • Miltenberger, R. J., K. A. Sukow, and P. J. Farnham. 1995. An E-box-mediated increase in cad transcription at the G1/S-phase boundary is suppressed by inhibitory c-Myc mutants. Mol. Cell. Biol. 15:2527–2535.
  • Min, S., and E. J. Taparowsky. 1992. v-Myc, but not Max, possesses domains that function in both transcription activation and cellular transformation. Oncogene 7:1531–1540.
  • Mukherjee, B., S. D. Morgenbesser, and R. A. DePinho. 1992. Myc family oncoproteins function through a common pathway to transform normal cells in culture: cross-interference by Max and trans-acting dominant mutants. Genes Dev. 6:1480–1492.
  • Nepveu, A., K. B. Marcu, A. I. Skoultchi, and H. M. Lachman. 1987. Contributions of transcriptional and post-transcriptional mechanisms to the regulation of c-myc expression in mouse erythroleukemia cells. Genes Dev. 1:938–945.
  • Pena, A., C. D. Reddy, S. Wu, N. J. Hickok, E. P. Reddy, G. Yumet, D. R. Soprano, and K. J. Soprano. 1993. Regulation of human ornithine decar-boxylase expression by the c-Myc:Max protein complex. J. Biol. Chem. 268:27277–27285.
  • Prendergast, G. C., R. Hopewell, R. J. Gorham, and E. B. Ziff. 1992. Biphasic effect of Max on Myc cotransformation activity and dependence on amino-and carboxy-terminal Max functions. Genes Dev. 6:2429–2439.
  • Prendergast, G. C., D. Lawe, and E. B. Ziff. 1991. Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation-sensitive DNA binding and Ras cotransformation. Cell 65:395–407.
  • Prochownik, E. V., and J. Kukowska. 1986. Deregulated expression of c-myc by murine erythroleukaemia cells prevents differentiation. Nature 322:848–850.
  • Prochownik, E. V., J. Kukowska, and C. Rodgers. 1988. c-myc antisense transcripts accelerate differentiation and inhibit G1 progression in murine erythroleukemia cells. Mol. Cell. Biol. 8:3683–3695.
  • Rao, G., L. Alland, P. Guida, N. Schreiber-Agus, K. Chen, L. Chin, J. M. Rochelle, M. F. Seldin, A. I. Skoultchi, and R. A. DePinho. 1996. Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression domain of the Myc antagonist Mxi1. Oncogene 12:1165–1172.
  • Reddy, C. D., P. Dasgupta, P. Saikumar, H. Dudek, F. Rauscher, and E. P. Reddy. 1992. Mutational analysis of Max: role of basic, helix-loop-helix/ leucine zipper domains in DNA binding, dimerization and regulation of Myc-mediated transcriptional activation. Oncogene 7:2085–2092.
  • Roussel, M. F., R. A. Ashmun, C. J. Sherr, R. N. Eisenman, and D. E. Ayer. 1996. Inhibition of cell proliferation by the Mad1 transcriptional repressor. Mol. Cell. Biol. 16:2796–2801.
  • Roy, B., and D. Reisman. 1995. Inducible expression of Mad accelerates growth arrest of serum deprived human glioblastoma cells. Cell Biol. Int. 19:307–313.
  • Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Schreiber-Agus, N., L. Chin, K. Chen, R. Torres, G. Rao, P. Guida, A. I. Skoultchi, and R. A. DePinho. 1995. An amino-terminal domain of Mxi1 mediates Anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor Sin3. Cell 80:777–786.
  • Shapiro, D. N., V. Valentine, L. Eagle, X. Yin, S. W. Morris, and E. V. Prochownik. 1994. Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-25. Genomics 23:282–285.
  • Spotts, G. D., and S. R. Hann. 1990. Enhanced translation and increased turnover of c-myc proteins occur during differentiation of murine erythro-leukemia cells. Mol. Cell. Biol. 10:3952–3964.
  • Stone, J., T. de Lange, G. Ramsay, E. Jakobovits, J. M. Bishop, H. Varmus, and W. Lee. 1987. Definition of region in human c-myc that are involved in transformation and nuclear localization. Mol. Cell. Biol. 7:1697–1709.
  • Vastrik, I., A. Kaipainen, T. Penttila, A. Lymboussakis, R. Alitalo, M. Par-vinen, and K. Alitalo. 1995. Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro. J. Cell Biol. 128:1197–1208.
  • Wagner, A. J., C. Meyers, A. Laimins, and N. Hay. 1993. c-Myc induces the expression and activity of ornithine decarboxylase. Cell Growth Differ. 4:879–883.
  • Zervos, A. S., J. Gyuris, and R. Brent. 1993. Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 72:223–232.

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