Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9.
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Arai S, Matsushita A, Du K, Yagi K, Okazaki Y, Kurokawa R
Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9.
FEBS Lett. 2007 Dec 11;581(29):5649-57. Epub 2007 Nov 20.
- PubMed ID
- 18022393 [ View in PubMed]
- Abstract
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.