PARP co-activates B-MYB through enhanced phosphorylation at cyclin/cdk2 sites

G. Santilli, M. N. Cervellera, T. K. Johnson, Robert E Lewis, S. Iacobelli, A. Sala

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18 Scopus citations


PARP is a multifunctional protein that can affect genome stability, transcription control, telomere length and cell death. Recently we have reported that PARP binds to and enhances B-MYB transactivating potential. B-MYB is a potentially oncogenic transcription factor involved in mammalian cell proliferation, survival and differentiation. B-MYB gene expression is growth regulated and B-MYB protein is phosphorylated during S phase by cyclin A or E/cdk2 kinase, resulting in augmented transactivating potential. Here we show that PARP induces phosphorylation of B-MYB protein at cdk2 phosphorylation sites, since a B-MYB protein with mutated cdk2 phosphorylation sites is refractory to PARP-induced phosphorylation and co-activation in mammalian cells. We propose that PARP functions as a B-MYB co-factor by promoting cyclin/cdk2-dependent B-MYB phosphorylation. These results highlight a novel role for PARP as a factor that integrates cyclin-dependent kinases signaling with gene transcription.

Original languageEnglish (US)
Pages (from-to)8167-8174
Number of pages8
Issue number57
Publication statusPublished - Jan 1 2001



  • Cell cycle
  • Promoter
  • Transcription
  • Transformation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

Cite this

Santilli, G., Cervellera, M. N., Johnson, T. K., Lewis, R. E., Iacobelli, S., & Sala, A. (2001). PARP co-activates B-MYB through enhanced phosphorylation at cyclin/cdk2 sites. Oncogene, 20(57), 8167-8174.