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c-Myc Function in Neoplasia pp 151–163Cite as

Max Association with Myc

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Part of the book series: Medical Intelligence Unit ((MIU.LANDES))

Abstract

Amajor breakthrough occurred in the study of transcriptional regulation by c-Myc when the partner protein, Max, was identified in 1991. It had been suspected that Myc partner proteins were necessary for Myc function because Myc possesses a dimerization domain that appears necessary for cell transformation. Although early studies indicated that Myc could homodimerize, it became rapidly apparent that homodimerization of c-Myc only occurs at high protein concentrations in vitro. Blackwood and Eisenman used a functional cloning strategy to identify two alternatively spliced Max mRNAs that encode proteins of 151 and 160 amino acids.1 The bHLHZip region of c-Myc fused to glutathioneS-transferase (GST) was used to screen a complementary DNA (cDNA) expression library. A bHLHZip protein, termed Max, was identified. Prendergast et al used a PCR strategy employing primers that matched conserved domains of Myc to identify Myn, the murine homolog of Max.2,3 Genes or cDNAs of max in other species, such as Xenopus, zebrafish and chicken, have been cloned as we11.4–7 The genomic structure of the chicken gene suggests that it contains a TATA-less promoter which consists of GC-rich sequences resembling binding sites for the transcriptional factor Sp1.4

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Authors and Affiliations

  1. School of Medicine, The Johns Hopkins University, Baltimore, Maryland, USA

    Chi V. Dang M.D., Ph.D. & Linda A. Lee M.D.

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  1. Chi V. Dang M.D., Ph.D.
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  2. Linda A. Lee M.D.
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© 1995 Springer-Verlag Berlin Heidelberg

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Dang, C.V., Lee, L.A. (1995). Max Association with Myc. In: c-Myc Function in Neoplasia. Medical Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-22681-0_8

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  • DOI: https://doi.org/10.1007/978-3-662-22681-0_8

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-22683-4

  • Online ISBN: 978-3-662-22681-0

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