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Myc and Max associate in vivo.

Blackwood, E M and Lüscher, B and Eisenman, R N (1992) Myc and Max associate in vivo. Genes & development, 6 (1). pp. 71-80. ISSN 0890-9369

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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.

Item Type: Article or Abstract
Additional Information: This article is freely available at the journal's website.
DOI: 10.1101/gad.6.1.71
PubMed ID: 1730411
Grant Numbers: T32 CA09437], ROl CA20525
Keywords or MeSH Headings: Basic-Leucine Zipper Transcription Factors; Binding Sites/genetics; Casein Kinases; DNA-Binding Proteins/metabolism; Gene Expression; Macromolecular Substances; Nuclear Proteins/metabolism; Oligodeoxyribonucleotides/genetics/metabolism; Peptide Mapping; Phosphorylation; Precipitin Tests; Protein Kinases/metabolism; Proto-Oncogene Proteins c-myc/metabolism; Recombinant Proteins/metabolism; Transcription Factors; Tumor Cells, Cultured;
Subjects: Molecules > Proteins > Transcription factors
Molecules > Proteins
Molecules > Genes > Oncogenes
Depositing User: Library Staff
Date Deposited: 03 Dec 2008 20:17
Last Modified: 07 May 2010 20:23

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