Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation

Roderick L. Beijersbergen, E. Marielle Hijmans, Liang Zhu, René Bernards

Research output: Contribution to journalArticle

118 Scopus citations

Abstract

The product of the c-myc proto-oncogene, c-Myc, is a sequence-specific DNA binding protein with an N-terminal transactivation domain and a C-terminal DNA binding domain. Several lines of evidence indicate that c-Myc activity is essential for normal cell cycle progression. Since the abundance of c-Myc during the cell cycle is constant, c-Myc's activity may be regulated at a post-translational level. We have shown previously that the N-terminus of c-Myc can form a specific complex with the product of the retinoblastoma gene, pRb, in vitro. These data suggested a model in which pRb, or pRb-related proteins, regulate c-Myc activity through direct binding. We show here that the pRb-related protein p107, but not pRb itself, forms a specific complex with the N-terminal transactivation domain of c-Myc in vivo. Binding of p107 to c-Myc causes a significant inhibition of c-Myc transactivation. Expression of c-Myc releases cells from a p107-induced growth arrest, but not from pRb-induced growth arrest. Our data suggest that p107 can control c-Myc activity through direct binding to the transactivation domain and that c-Myc is a target for p107-mediated growth suppression.

Original languageEnglish (US)
Pages (from-to)4080-4086
Number of pages7
JournalEMBO Journal
Volume13
Issue number17
StatePublished - Sep 19 1994
Externally publishedYes

Keywords

  • Transactivation
  • c-Myc
  • p107
  • pRb

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Fingerprint Dive into the research topics of 'Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation'. Together they form a unique fingerprint.

  • Cite this