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Pim-1 phosphorylates the DNA binding domain of c-Myb

Louise M Winn1, Wanli Lei, Scott A Ness

  • 1Department of Pharmacology and Toxicology, Botterell Hall, Queen's University, Kingston, Ontario K7L 3N6, Canada. winnl@biology.queensu.ca

Cell Cycle (Georgetown, Tex.)
|May 8, 2003
PubMed

Insights

The serine/threonine protein kinase Pim-1 directly interacts with and phosphorylates the Myb DNA binding domain of c-Myb and A-Myb transcription factors, regulating their activity.

Area of Science:

  • Molecular Biology
  • Oncology
  • Gene Regulation

Background:

  • The c-Myb transcription factor is crucial for cell differentiation and proliferation.
  • Its oncogenic activity is tightly regulated by complex cellular mechanisms.
  • The serine/threonine protein kinase Pim-1 is known to modulate c-Myb transcriptional activity.

Purpose of the Study:

  • To investigate the molecular mechanism by which Pim-1 regulates c-Myb and related transcription factors.
  • To determine if Pim-1 directly interacts with and phosphorylates c-Myb and A-Myb.

Main Methods:

  • Co-immunoprecipitation assays to detect protein-protein interactions in cellular and in vitro settings.
  • In vitro kinase assays to assess phosphorylation of Myb proteins by Pim-1.
  • Analysis of interactions with the conserved Myb DNA binding domain.

Main Results:

  • Pim-1 directly interacts with both c-Myb and A-Myb transcription factors.
  • These interactions occur via the highly conserved Myb DNA binding domain.
  • Pim-1 phosphorylates the Myb DNA binding domain of these transcription factors, both in cells and in vitro.

Conclusions:

  • Pim-1 directly binds to and phosphorylates the DNA binding domain of c-Myb and A-Myb.
  • This direct phosphorylation by Pim-1 is a key mechanism for regulating Myb protein activity.
  • Findings provide insight into the regulation of oncogenic transcription factors.

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