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Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity

D E Ayer1, L Kretzner, R N Eisenman

  • 1Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104.

Cell
|January 29, 1993
PubMed

Insights

Researchers discovered a new protein, Mad, which partners with Max. This Mad-Max complex, like Myc-Max, binds DNA but has opposing functions, revealing Max

Area of Science:

  • Molecular Biology
  • Genetics
  • Protein Interactions

Background:

  • Myc proteins are transcription factors that heterodimerize with Max.
  • The role of Max in mediating functions of other regulatory proteins is not fully understood.

Purpose of the Study:

  • To identify novel proteins that interact with Max.
  • To characterize the function and DNA-binding properties of Max-interacting proteins.

Main Methods:

  • Screening of a lambda gt11 expression library using radiolabeled Max protein.
  • In vitro binding assays to assess protein-protein interactions.
  • In vivo transactivation assays to evaluate transcriptional activity.

Main Results:

  • Identification of a new bHLH-Zip protein, Mad, that binds to Max.
  • Formation of Mad-Max heterodimers with DNA-binding properties similar to Myc-Max.
  • Both Myc-Max and Mad-Max complexes are favored over Max homodimers and are unaffected by CKII phosphorylation.
  • Mad-Max and Myc-Max complexes exhibit opposing functions in transcription.

Conclusions:

  • Max is a central mediator in a network of transcription factors involving Myc and Mad.
  • Mad represents a novel functional partner for Max, with opposing transcriptional roles to Myc.

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