Regulation of Cell Growth by the Myc-Max-Mad Network: Role of Mad Proteins and YY1
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.
KeywordsTATA Binding Protein Reporter Gene Construct Human Brain Tumor Cell
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- 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
- 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
- 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