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Gene Review

Max  -  MYC associated factor X

Rattus norvegicus

Synonyms: Myc-associated factor X, Protein max
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Disease relevance of Max

  • We also analyzed the effects of Myc and Max ectopic expression on the clonogenic growth of the rat hepatoma cells [1].
  • These data support the hypothesis that N-Myc affects neuroblastoma gene expression through the formation of a DNA-binding heterodimeric complex with Max in vivo [2].
  • Reintroduction of max into PC12 cells results in repression of E-box-dependent transcription and a reduction in growth rate, which may explain the loss of Max expression either during the growth of the pheochromocytoma or in subsequent passage of the PC12 cell line in vitro [3].

High impact information on Max

  • This delta Max protein retained the ability to bind to the CACGTG motif in a complex with c-Myc but lacks the nuclear localization signal and the putative regulatory domain of Max [4].
  • When tested in a myc-ras cotransformation assay in rat embryo fibroblasts, Max suppressed, whereas delta Max enhanced, transformation [4].
  • Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation [4].
  • Myc heterodimerizes with a partner protein termed Max; the heterodimeric complex binds to CAC(G/A)TG (E-box) sequences and activates transcription from these sites [5].
  • The c-Myc protein induces cell cycle progression and apoptosis through dimerization with Max [6].

Biological context of Max


Anatomical context of Max


Associations of Max with chemical compounds

  • Max activity is affected by phosphorylation at two NH2-terminal sites [14].
  • Replacing these serine by alanine residues and comparing the wild type with the mutant Max proteins in transactivation assays did not reveal any significant differences [15].
  • In this study, the glucose-mediated induction of L-type pyruvate kinase and glucose-6-phosphatase mRNA levels was diminished by maneuvers involving recombinant adenoviral vectors that interfere with (i) c-Myc protein levels by antisense expression or (ii) c-Myc function through a dominant-negative Max protein [16].

Physical interactions of Max

  • Max is a basic-helix-loop-helix-leucine zipper protein capable of forming sequence-specific DNA binding complexes with Myc proteins [4].

Other interactions of Max

  • Neutralization with anti-adrenomedullin antiserum or blockade with a CGRP receptor antagonist, CGRP(8-37), reduced Max mRNA levels in growing endothelial cells and enhanced apoptosis after serum starvation [12].
  • By using complementary leucine zipper mutants (termed MycEG and MaxEG), which dimerize efficiently with each other but not with their wild-type partners, we demonstrate that both cell cycle progression and apoptosis in nontransformed rodent fibroblasts are induced by Myc-Max dimers [6].

Analytical, diagnostic and therapeutic context of Max

  • By means of sequential immunoprecipitation of chromatin using anti-Max and anti-Myc antibodies, we have identified a Myc-regulated gene and genomic sites occupied by Myc-Max in vivo [17].
  • In addition to the previously identified Max and delta Max proteins, sequence analysis of a 3.5-kb mRNA form predicted a protein that resembles delta Max in structure [18].


  1. Kinetics of myc-max-mad gene expression during hepatocyte proliferation in vivo: Differential regulation of mad family and stress-mediated induction of c-myc. Mauleon, I., Lombard, M.N., Muñoz-Alonso, M.J., Cañelles, M., Leon, J. Mol. Carcinog. (2004) [Pubmed]
  2. A dominant-negative mutant of Max that inhibits sequence-specific DNA binding by Myc proteins. Billaud, M., Isselbacher, K.J., Bernards, R. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  3. The nerve growth factor-responsive PC12 cell line does not express the Myc dimerization partner Max. Hopewell, R., Ziff, E.B. Mol. Cell. Biol. (1995) [Pubmed]
  4. Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation. Mäkelä, T.P., Koskinen, P.J., Västrik, I., Alitalo, K. Science (1992) [Pubmed]
  5. Discrimination between different E-box-binding proteins at an endogenous target gene of c-myc. Desbarats, L., Gaubatz, S., Eilers, M. Genes Dev. (1996) [Pubmed]
  6. The c-Myc protein induces cell cycle progression and apoptosis through dimerization with Max. Amati, B., Littlewood, T.D., Evan, G.I., Land, H. EMBO J. (1993) [Pubmed]
  7. Myc drives apoptosis in PC12 cells in the absence of Max. Wert, M., Kennedy, S., Palfrey, H.C., Hay, N. Oncogene (2001) [Pubmed]
  8. Repression of in vivo growth of Myc/Ras transformed tumor cells by Mad1. Cerni, C., Skrzypek, B., Popov, N., Sasgary, S., Schmidt, G., Larsson, L.G., Lüscher, B., Henriksson, M. Oncogene (2002) [Pubmed]
  9. c-Myc does not require max for transcriptional activity in PC-12 cells. Ribon, V., Leff, T., Saltiel, A.R. Mol. Cell. Neurosci. (1994) [Pubmed]
  10. c-Myc and Max interactions in quiescent and mitogen-stimulated primary hepatocytes. Skouteris, G.G., Schröder, C.H. Exp. Cell Res. (1996) [Pubmed]
  11. Molecular cloning and sequencing of rat Max cDNA: castration-induced expression of the 2 kb transcript in male accessory sex organs of rats. Izawa, M. Biochim. Biophys. Acta (1993) [Pubmed]
  12. Induction of max by adrenomedullin and calcitonin gene-related peptide antagonizes endothelial apoptosis. Shichiri, M., Kato, H., Doi, M., Marumo, F., Hirata, Y. Mol. Endocrinol. (1999) [Pubmed]
  13. Expression and subcellular localization of the Myc superfamily proteins: c-Myc, Max, Mad1 and Mxi1 in the epiphyseal plate cartilage chondrocytes of growing rats. Wang, Y., Toury, R., Hauchecorne, M., Balmain, N. Cell. Mol. Biol. (Noisy-le-grand) (1997) [Pubmed]
  14. Max activity is affected by phosphorylation at two NH2-terminal sites. Koskinen, P.J., Västrik, I., Mäkelä, T.P., Eisenman, R.N., Alitalo, K. Cell Growth Differ. (1994) [Pubmed]
  15. Regulation of transcription factors c-Myc, Max, and c-Myb by casein kinase II. Bousset, K., Oelgeschläger, M.H., Henriksson, M., Schreek, S., Burkhardt, H., Litchfield, D.W., Lüscher-Firzlaff, J.M., Lüscher, B. Cell. Mol. Biol. Res. (1994) [Pubmed]
  16. c-Myc is required for the glucose-mediated induction of metabolic enzyme genes. Collier, J.J., Doan, T.T., Daniels, M.C., Schurr, J.R., Kolls, J.K., Scott, D.K. J. Biol. Chem. (2003) [Pubmed]
  17. Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo. Grandori, C., Mac, J., Siëbelt, F., Ayer, D.E., Eisenman, R.N. EMBO J. (1996) [Pubmed]
  18. Alternative mRNA forms and open reading frames of the max gene. Västrik, I., Koskinen, P.J., Alitalo, R., Mäkelä, T.P. Oncogene (1993) [Pubmed]
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