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v-Myc inhibits C/EBPbeta activity by preventing C/EBPbeta-induced phosphorylation of the co-activator p300

S Steinmann1, K Schulte, K Beck

  • 1Institut für Biochemie, Westfälische-Wilhelms-Universität Münster, Münster, Germany.

Oncogene
|May 19, 2009
PubMed

Insights

v-Myc suppresses cell differentiation by interfering with C/EBPbeta transcription factors. It prevents the phosphorylation of p300 by HIPK2, a crucial step in regulating gene transcription.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Myc proteins regulate cell proliferation, differentiation, and apoptosis.
  • C/EBP transcription factors are vital for cell differentiation and are targeted by Myc proteins.
  • v-Myc and c-Myc suppress myeloid and fat cell differentiation.

Purpose of the Study:

  • To elucidate the mechanism by which v-Myc suppresses C/EBPbeta activity.
  • To identify how v-Myc interferes with the function of C/EBPbeta transcription factors.

Main Methods:

  • Investigated the interaction between v-Myc and C/EBPbeta.
  • Analyzed the role of p300 co-activator and its phosphorylation.
  • Identified the specific protein kinase involved in C/EBPbeta-induced p300 phosphorylation.

Main Results:

  • v-Myc binds to the aminoterminal domain of C/EBPbeta.
  • v-Myc prevents C/EBPbeta-induced phosphorylation of p300.
  • Homeo-domain interacting protein kinase 2 (HIPK2) was identified as the kinase responsible for p300 phosphorylation.
  • v-Myc displaces HIPK2 from the C/EBPbeta-p300 complex.

Conclusions:

  • v-Myc employs a novel mechanism of transcriptional suppression by modulating C/EBPbeta-induced p300 phosphorylation.
  • Disruption of the C/EBPbeta-p300-HIPK2 complex by v-Myc inhibits C/EBPbeta transcriptional activity.

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