Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo

The Journal of Biological Chemistry
Eun-Joo KimSoo-Jong Um

Abstract

To study the biological role of p73 alpha, a member of the p53 tumor suppressor family, we performed a yeast two-hybrid screen of a human cDNA library. Using a p73 alpha fragment consisting of amino acids 49-636 as bait, we found that p73 alpha is functionally associated with the human homologue of mouse and hamster homeodomain-interacting protein kinase 2 (HIPK2). The hamster homologue, also known as haHIPK2 or PKM, was used for further characterization of interactions between HIPK2 and members of the p53 protein family. Systematic yeast two-hybrid assays indicated a physical interaction between the oligomerization domains of p73 alpha and p53 (amino acid regions 345-380 and 319-360, respectively) and amino acid region 812-907 of haHIPK2. This region of haHIPK2 includes a PEST sequence, an Ubc9-binding domain, and a partial speckle retention sequence and is identical to amino acid residues 846-941 of human HIPK2 (hHIPK2). The interaction was confirmed by glutathione S-transferase pull-down assays in vitro and immunoprecipitation assays in vivo. HIPK2 colocalized with p73 and p53 in nuclear bodies, as shown by confocal microscopy. Overexpression of HIPK2 stabilized the p53 protein and greatly increased the p73- and p53-induced ...Continue Reading

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