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Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases

Yuexing Zhang1, Nicholas Woodford, Xianmin Xia

  • 1Greenebaum Cancer Center, University of Maryland, Baltimore, MD 21201, USA.

Nucleic Acids Research
|April 12, 2003
PubMed

Insights

ErbB3 binding protein 1 (Ebp1) inhibits cancer cell proliferation by repressing E2F target genes. This repression involves recruiting histone deacetylase (HDAC) activity to specific DNA elements.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Cycle Regulation

Background:

  • ErbB3 binding protein 1 (Ebp1) is a proliferation-associated protein.
  • Ebp1 inhibits proliferation and induces differentiation in ErbB-positive breast and prostate cancer cells.
  • Ebp1 interacts with the retinoblastoma protein (Rb) to inhibit E2F1-regulated gene transcription.

Purpose of the Study:

  • To investigate the broader transcriptional regulatory role of Ebp1.
  • To elucidate the mechanism underlying Ebp1-mediated transcriptional repression.
  • To determine if Ebp1's repression activity is dependent on histone deacetylase (HDAC) recruitment.

Main Methods:

  • Ebp1's effect on various E2F-regulated reporter genes and endogenous genes was assessed.
  • Experiments were conducted in both Rb-positive and Rb-null cell lines.
  • GAL4-Ebp1 fusion protein assays and in vitro binding assays with HDACs were performed.

Main Results:

  • Ebp1 repressed transcription of multiple E2F-regulated genes, independent of Rb status.
  • Transcriptional repression was dependent on an E2F1 consensus element.
  • Ebp1's C-terminal region bound HDAC activity, and HDAC inhibitors reduced repression.

Conclusions:

  • Ebp1 functions as a transcriptional repressor of E2F-regulated promoters.
  • Ebp1 recruits HDAC activity to mediate transcriptional repression.
  • This mechanism highlights a novel role for Ebp1 in cell cycle control and cancer.

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