MAX (gene)

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Protein-coding gene in humans

title: "MAX (gene)" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["transcription-factors"] description: "Protein-coding gene in humans" topic_path: "arts/film" source: "https://en.wikipedia.org/wiki/MAX_(gene)" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in humans ::

MAX (also known as myc-associated factor X) is a gene that in humans encodes the MAX transcription factor.

Function

The protein product of MAX contains the basic helix-loop-helix and leucine zipper motifs. It is therefore included in the bHLHZ family of transcription factors. It is able to form homodimers with other MAX proteins and heterodimers with other transcription factors, including Mad, Mxl1 and Myc. The homodimers and heterodimers compete for a common DNA target site (the E-box) in a gene promoter zone. Rearrangement of dimers (e.g., Mad:Max, Max:Myc) provides a system of transcriptional regulation with greater diversity of gene targets. Max must dimerise in order to be biologically active.

Transcriptionally active hetero- and homodimers involving Max can promote cell proliferation as well as apoptosis.

Interactions

The protein product of Max has been shown to interact with:

Clinical relevance

This gene has been shown mutated in cases of hereditary pheochromocytoma. More recently the Max gene becomes mutated and becomes inactivated in small cell lung cancer (SCLC). This is mutually exclusive with alterations at Myc and BRG1, the latter coding for an ATPase of the SWI/SNF complex. It was demonstrated that the BRG1 product regulates the expression of Max through direct recruitment to the Max promoter region, and that depletion of BRG1 strongly hinders cell growth, specifically in Max-deficient cells, suggesting that the two together cause synthetic lethality. Furthermore, Max required BRG1 to activate neuroendocrine transcriptional programs and to up-regulate Myc targets, such as glycolytic-related genes.

References

References

  1. (April 1992). "Expression, regulation, and chromosomal localization of the Max gene". Proceedings of the National Academy of Sciences of the United States of America.
  2. "Entrez Gene: MAX MYC associated factor X".
  3. (March 2010). "Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA". Biochemistry.
  4. (February 1994). "Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death". Current Opinion in Genetics & Development.
  5. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology.
  6. (January 2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc". Molecular and Cellular Biology.
  7. (August 1998). "The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins". Cell.
  8. (May 1999). "c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function". Nature Genetics.
  9. (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene.
  10. (February 2003). "Interactions of the DNA mismatch repair proteins MLH1 and MSH2 with c-MYC and MAX". Oncogene.
  11. (October 2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". Proceedings of the National Academy of Sciences of the United States of America.
  12. (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene.
  13. (January 2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell.
  14. (January 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell.
  15. (December 1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". The Journal of Biological Chemistry.
  16. (May 1997). "Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor". The EMBO Journal.
  17. (April 1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene.
  18. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature.
  19. (March 1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science.
  20. (July 1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Molecular and Cellular Biology.
  21. (June 2011). "Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma". Nature Genetics.
  22. (March 2014). "MAX inactivation in small cell lung cancer disrupts MYC-SWI/SNF programs and is synthetic lethal with BRG1". Cancer Discovery.

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transcription-factors