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Updated: Jun 21, 2026
14:47
Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry
Published on: May 17, 2016
HIPK1 interacts with c-Myb and modulates its activity through phosphorylation
Vilborg Matre1, Oddmund Nordgård, Anne Hege Alm-Kristiansen
1Department of Molecular Biosciences, University of Oslo, Norway.
Biochemical and Biophysical Research Communications
|August 4, 2009
Summary
The nuclear kinase HIPK1 interacts with the c-Myb transcription factor, a key regulator of blood cell development. HIPK1 phosphorylates c-Myb, inhibiting its ability to activate target genes involved in haematopoiesis.
Area of Science:
- Molecular Biology
- Cell Biology
- Hematology
Background:
- The transcription factor v-Myb induces myeloid leukaemias.
- Cellular c-Myb is critical for regulating haematopoiesis (blood cell formation).
Purpose of the Study:
- To identify novel interaction partners of human c-Myb.
- To elucidate the functional relationship between c-Myb and its interacting partners in haematopoiesis.
Main Methods:
- Yeast two-hybrid (Y2H) screening to identify protein interactions.
- Co-transfection assays to study protein localization.
- In vivo and in vitro phosphorylation assays.
- Functional assays using the mim-1 target gene.
Main Results:
- HIPK1 was identified as a binding partner for c-Myb.
- Interaction involves specific regions of both HIPK1 and c-Myb.
- HIPK1 and c-Myb co-localize in nuclear foci.
- HIPK1 phosphorylates c-Myb in its negative regulatory domain.
- HIPK1 represses c-Myb's activation of the mim-1 gene in hematopoietic cells.
Conclusions:
- HIPK1 is a novel kinase that interacts with and regulates the activity of the c-Myb transcription factor.
- This interaction provides a new link between kinase activity and the regulation of haematopoiesis.
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