Abstract
Members of the myc family of nuclear proto-oncogenes (c-, N- and L-myc) play central roles in the control of normal growth and development and in genetic pathways linked to cellular transformation and apoptotic cell death (for reviews see [19, 40]). Accumulating structural, biochemical, and genetic evidence affords the view that the function of Myc family oncoproteins in these diverse processes relates in part to their roles as sequence-specific transcription factors (for reviews see [31, 58]). Myc family proteins possess a multi-functional amino-terminal domain with transactivation potential [32], a region rich in basic amino acid residues responsible for sequence-specific DNA binding activity to the E-box consensus CACGTG [8], and a carboxy-terminal α-helical domain required for dimerization with another basic region helix-loop-helix/leucine zipper (bHLH/LZ) protein, Max [9, 43]. Many of the biochemical and biological activities of Myc appear to be highly dependent upon its association with Max [1, 2, 9, 35, 43). In addition to its key role as an obligate partner in transactivation-competent Myc/Max complexes, Max may also repress Myc-responsive genes through the formation of transactivation-inert complexes that are capable of binding the Myc/Max recognition sequence [5, 10, 33, 35, 39, 41, 44, 65]. These complexes include Max/Max homodimers, and the heterodimers Mad/Max [5, 29] and Mxil/Max [65].
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Schreiber-Agus, N. et al. (1997). A Biochemical and Biological Analysis of Myc Superfamily Interactions. In: Potter, M., Melchers, F. (eds) C-Myc in B-Cell Neoplasia. Current Topics in Microbiology and Immunology, vol 224. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60801-8_16
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DOI: https://doi.org/10.1007/978-3-642-60801-8_16
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