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Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9

We describe here the cloning and characterization of a novel mouse homeodomain-interacting protein kinase (HIPK)-like gene, Hipk4. Hipk4 is expressed in lung and in white adipose tissue and encodes a 616 amino acid protein that includes a serine/threonine kinase domain. We demonstrate that HIPK4 cou...

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Bibliographic Details
Published in:FEBS letters 2007-12, Vol.581 (29), p.5649-5657
Main Authors: Arai, Shigeki, Matsushita, Akio, Du, Kun, Yagi, Ken, Okazaki, Yasushi, Kurokawa, Riki
Format: Article
Language:English
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Summary:We describe here the cloning and characterization of a novel mouse homeodomain-interacting protein kinase (HIPK)-like gene, Hipk4. Hipk4 is expressed in lung and in white adipose tissue and encodes a 616 amino acid protein that includes a serine/threonine kinase domain. We demonstrate that HIPK4 could phosphorylate human p53 protein at serine 9, both in vitro and in vivo. Among known p53-responsive promoters, activity of the human survivin promoter, which is repressed by p53, was decreased by HIPK4 in p53 functional A549 cells. Human BCL2-associated X protein-promoter activity was not affected. These findings suggest that phosphorylation of p53 at serine 9 is important for p53 mediated transcriptional repression.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.11.022