Myc and Max associate in vivo

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

Research output: Contribution to journalArticle

297 Citations (Scopus)

Abstract

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
Volume6
Issue number1
DOIs
StatePublished - Jan 1 1992

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Casein Kinase II
Proteins
Nuclear Proteins
Mitogens
Oligonucleotides
Anti-Idiotypic Antibodies
DNA
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology

Cite this

Blackwood, E. M. ; Luscher, B. ; Eisenman, R. N. / Myc and Max associate in vivo. In: Genes and Development. 1992 ; Vol. 6, No. 1. pp. 71-80.
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Blackwood, EM, Luscher, B & Eisenman, RN 1992, 'Myc and Max associate in vivo', Genes and Development, vol. 6, no. 1, pp. 71-80. https://doi.org/10.1101/gad.6.1.71

Myc and Max associate in vivo. / Blackwood, E. M.; Luscher, B.; Eisenman, R. N.

In: Genes and Development, Vol. 6, No. 1, 01.01.1992, p. 71-80.

Research output: Contribution to journalArticle

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