HIPK1 interacts with c-Myb and modulates its activity through phosphorylation.
Article Details
- CitationCopy to clipboard
Matre V, Nordgard O, Alm-Kristiansen AH, Ledsaak M, Gabrielsen OS
HIPK1 interacts with c-Myb and modulates its activity through phosphorylation.
Biochem Biophys Res Commun. 2009 Oct 9;388(1):150-4. doi: 10.1016/j.bbrc.2009.07.139. Epub 2009 Jul 30.
- PubMed ID
- 19646965 [ View in PubMed]
- 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.