Advertisement

Regulation of Cell Growth by the Myc-Max-Mad Network: Role of Mad Proteins and YY1

  • M. Austen
  • C. Cerni
  • M. Henriksson
  • S. Hilfenhaus
  • J. M. Lüscher-Firzlaff
  • A. Menkel
  • C. Seelos
  • A. Sommer
  • B. Lüscher
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 224)

Abstract

Since the discovery of the c-Myc dimerization partner Max (Blackwood and Eisenman 1991; Prendergast et al. 1991) a startling number of proteins capable to interact directly or indirectly with c-Myc and/or Max have been described (for review see Marcu et al. 1992; Henriksson and Lüscher 1996). It has become evident that at the center of this network lies Max which on one hand forms heterodimers with the Myc family of proteins, including c-, N-, and L-Myc and on the other hand heterodimerizes with proteins of the Mad family, including Mad1, Mxi1 (or Mad2), Mad3, and Mad4. In addition Max has also the ability to form homodimers. Thus Max is the true center of this array of proteins which we will refer to as the Myc/Max/Mad network.

Keywords

TATA Binding Protein Reporter Gene Construct Human Brain Tumor Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Amati, B., Brooks, M. W., Levy, N., Littlewood, T. D., Evan, G. L, and Land, H. (1993). Oncogenic activity of the c-Myc protein requires dimerization with Max. Cell 72, 233–245.PubMedCrossRefGoogle Scholar
  2. Amati, B., Dalton, S., Brooks, M. W., Littlewood, T. D., Evan, G. I., and Land, H. (1992). Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max. Nature 359, 423–426.PubMedCrossRefGoogle Scholar
  3. Austen, M., Lüscher, B., and Lüscher-Firzlaff, J. M. (1997). Characterization of the transcriptional regulator YY1: the bipartite transactivation doamin is independet of interaction with TBP, TFIIB, TAFII55, or CBP. J. Biol. Chem. in press.Google Scholar
  4. Ayer, D. E., and Eisenman, R. N. (1993). A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. Genes Dev. 7, 2110–2119.PubMedCrossRefGoogle Scholar
  5. Ayer, D. E., Kretzner, L., and Eisenman, R. N. (1993). Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72, 211–222.PubMedCrossRefGoogle Scholar
  6. Beijersbergen, R. L., Hijmans, E. M., Zhu, L., and Bernards, R. (1994). Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation. EMBO J. 13, 4080–4086.PubMedCentralPubMedGoogle Scholar
  7. Blackwood, E. M., and Eisenman, R. N. (1991). Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251, 1211–1217.PubMedCrossRefGoogle Scholar
  8. Cerni, C, Bousset, K., Seelos, C, Burkhardt, H., Henriksson, M., and Lüscher, B. (1995). Differential effects by Mad and Max on transformation by cellular and viral oncoproteins. Oncogene 11, 587–596.PubMedGoogle Scholar
  9. Chen, J., Willingham, T., Margraf, L. R., Schreiber-Agus, N., DePinho, R. A., and Nisen, P. D. (1995). Effects of the Myc oncogene antagonist, Mad, on proliferation, cell cycling and the malignant phenotype of human brain tumor cells. Nature Medicine 1, 638–643.PubMedCrossRefGoogle Scholar
  10. Gu, W., Bhatia, K., Magrath, I. T., Dang, C. V., and Dalla-Favera, R. (1994). Binding and suppression of the Myc transcriptional activation domain by p107. Science 264, 251–254.PubMedCrossRefGoogle Scholar
  11. Hahn, S. (1992). The yin and the yang of mammalian transcription. Curr. Biol. 2, 152–154.PubMedCrossRefGoogle Scholar
  12. Henriksson, M., and Lüscher, B. (1996). Proteins of the Myc network: Essential regulators of cell growth and differentiation. Adv. Cancer Res. 68, 109–182.PubMedCrossRefGoogle Scholar
  13. Hurlin, P. J., Quéva, C, Koskinen, P. J., Steingrimsson, E., Ayer, D. E., Copeland, N. G., Jenkins, N. A., and Eisenman, R. N. (1995a). 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.PubMedCentralPubMedGoogle Scholar
  14. Hurlin, P. J., Foley, K. P., Ayer, D. E., Eisenman, R. N., Hanahan, D., and Arbeit, J. M. (1995b). Regulation of Myc and Mad during epidermal differentiation and HPV-associated tumorigenesis. Oncogene 11,2487–2501.PubMedGoogle Scholar
  15. Koskinen, P. J., Ayer, D. E., and Eisenman, R. N. (1995). Mad repression of Myc-Ras cotransformation is mediated by multiple protein-protein interactions. Cell Growth Diff., 6, 623–629.PubMedGoogle Scholar
  16. Lahoz, E. G., Xu, L., Schreiber-Agus, N., and DePinho, R. A. (1994). Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1. Proc. Natl. Acad. Sci. USA 91, 5503–5507.PubMedCentralPubMedCrossRefGoogle Scholar
  17. Lüscher, B., Austen, M., Sommer, A., Hilfenhaus, S., and Henriksson, M. (1996). Transcriptional regulation by the Myc-Max-Mad network. In: Papavassiliou AG (ed) Transcription factors in Eukaryotes. RG Land Company, in press.Google Scholar
  18. Marcu, K. B., Bossone, S. A., and Patel, A. J. (1992). myc function and regulation. Annu. Rev. Biochem. 61, 809–860.PubMedCrossRefGoogle Scholar
  19. Packham, G., and Cleveland, J. L. (1995). c-Myc and apoptosis. Biochem. Biophys. Acta 1242, 11–28.PubMedGoogle Scholar
  20. Prendergast, G. C, Lawe, D., and Ziff, E. B. (1991). Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation-sensitive DNA binding and Ras cotransformation. Cell 65, 395–407.PubMedCrossRefGoogle Scholar
  21. Roussel, M. F., Ashmun, R. A., Sherr, C. J., Eisenman, R. N., and Ayer, D. E. (1996). Inhibition of cell proliferation by the Mad1 transcriptional repressor. Mol. Cell. Biol. 16, 2796–2801.PubMedCentralPubMedGoogle Scholar
  22. Sakamuro, D., Elliott, J., Wechsler-Reya, R., and Prendergast, G. C. (1996). Bin1 is a novel Myc-interacting protein with features of a tumour suppressor. Nature Genet. 14, 69–77.PubMedCrossRefGoogle Scholar
  23. Shrivastava, A., and Calame, K. (1994). An analysis of genes regulated by the multi-functional transcriptional regulator Yin Yang-1. Nuc1. Acids Res. 22, 5151–5155.CrossRefGoogle Scholar
  24. Shrivastava, A., Saleque, S., Kalpana, G. V., Artandi, S., Goff, S. P., and Calame, K. (1993). Inhibition of transcriptional regulator Yin-Yang-1 by association with c-Myc. Science 262, 1889–1892.PubMedCrossRefGoogle Scholar
  25. Shrivastava, A., Yu, J., Artandi, S., and Caíame, K. (1996). YY1 and c-Myc associate in vivo in a manner that depends on c-Myc levels. Proc. Natl. Acad. Sci. USA 93, 10638–10641.PubMedCentralPubMedCrossRefGoogle Scholar
  26. Vastrik, I., Kaipainen, A., Penttilä, T.-L., Lymboussakis, A., Alitalo, R., Parvinen, M., and Alitalo, K. (1995a). Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro. J. Cell Biol. 128, 1197–1208.PubMedCrossRefGoogle Scholar
  27. Zervos, A. S., Gyuris, J., and Brent, R. (1993). Mxil, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 72, 223–232.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1997

Authors and Affiliations

  • M. Austen
    • 1
  • C. Cerni
    • 2
  • M. Henriksson
    • 1
  • S. Hilfenhaus
    • 1
  • J. M. Lüscher-Firzlaff
    • 1
  • A. Menkel
    • 1
  • C. Seelos
    • 2
  • A. Sommer
    • 1
  • B. Lüscher
    • 1
  1. 1.Institut für MolekularbiologieMedizinische Hochschule HannoverHannoverGermany
  2. 2.Institut für TumorbiologieUniversität WienAustria

Personalised recommendations