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    Biochem Biophys Res Commun. 2009 Oct 9;388(1):150-4. Epub 2009 Jul 30.

    HIPK1 interacts with c-Myb and modulates its activity through phosphorylation.

    Matre V, Nordgård O, Alm-Kristiansen AH, Ledsaak M, Gabrielsen OS.

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    Department of Molecular Biosciences, University of Oslo, Norway.

    Abstract

    The transcription factor v-Myb is a potent inducer of myeloid leukaemias, and its cellular homologue c-Myb plays a crucial role in the regulation of haematopoiesis. In a yeast two-hybrid (Y2H) screening we identified the nuclear kinase HIPK1 as an interaction partner for human c-Myb. The interaction involves a C-terminal region of HIPK1, while a bipartite interaction surface was identified in c-Myb, including regions in its N-terminal DNA-binding domain as well as in its C-terminal region. HIPK1 and c-Myb co-localize in distinct nuclear foci upon co-transfection. c-Myb appears to be phosphorylated by HIPK1 in its negative regulatory domain as supported by both in vivo and in vitro data. A functional assay revealed that HIPK1 repressed the ability of c-Myb to activate a chromatin embedded target gene, mim-1, in haematopoetic cells. Our findings point to a novel link between an important kinase and a key regulator of haematopoiesis.

    PMID:
    19646965
    [PubMed - indexed for MEDLINE]

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