Myc and Max associate in vivo

E. M. Blackwood, B. Luscher, R. N. Eisenman

Research output: Contribution to journalArticlepeer-review

317 Scopus citations


Max is a helix-loop-helix zipper protein that associates in vitro with Myc family proteins to form a sequence-specific DNA-binding complex. We show here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max. This complex possesses specific DNA-binding activity for CACGTG-containing oligonucleotides. Although Max itself is a highly stable protein, Myc is rapidly degraded during or after its association with Max. In vivo Max is shown to be a nuclear protein phosphorylated by casein kinase II, and alternatively spliced forms of Max are expressed in cells. Furthermore, the levels of Max expression are equivalent in quiescent, mitogen-stimulated, and cycling cells. We conclude that the highly regulated rate of Myc biosynthesis is likely to be a limiting step in the formation of Myc:Max complexes.

Original languageEnglish (US)
Pages (from-to)71-80
Number of pages10
JournalGenes and Development
Issue number1
StatePublished - 1992

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology


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