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Cell Cycle. 2003 May-Jun;2(3):258-62.

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

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

Abstract

The c-Myb transcription factor regulates cellular differentiation and proliferation and is regulated by complex mechanisms that control its repressed oncogenic activity. The transcriptional activity of c-Myb is regulated by the serine/threonine protein kinase Pim-1. Here, we show that Pim-1 is able to interact with c-Myb and the closely related transcription factor A-Myb, via direct interactions with the highly conserved Myb DNA binding domain. Pim-1 associated with Myb both in cells and in vitro, and phosphorylated the Myb DNA binding domain, suggesting that it regulates Myb protein activity by direct phosphorylation.

PMID:
12734436
[PubMed - indexed for MEDLINE]
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