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J. Biol. Chem., Vol. 278, Issue 39, 37722-37729, September 26, 2003

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TP53INP1s and Homeodomain-interacting Protein Kinase-2 (HIPK2) Are Partners in Regulating p53 Activity^*

Richard Tomasini  , Amina Azizi Samir  ¶, Alice Carrier ||, Daniel Isnardon **, Barbara Cecchinelli , Silvia Soddu , Bernard Malissen ||, Jean-Charles Dagorn , Juan L. Iovanna  and Nelson J. Dusetti  

From the Centre de Recherche INSERM, EMI 0116, 163 Avenue de Luminy, BP172, Parc Scientifique et Technologique de Luminy, 13009 Marseille, France, ^||Centre d'Immunologie INSERM-CNRS de Marseille-Luminy, Case 906, Parc Scientifique et Technologique de Luminy, 13288 Marseille CEDEX 9, France, ^**Microscopie et Traitement des Images, Institut Paoli-Calmettes, 232 Boulevard Sainte Marguerite, 13009 Marseille, France, and Molecular Oncogenesis Laboratory, Regina Elena Cancer Institute, Via delle Messi d'Oro 156, 00158 Rome, Italy

The TP53INP1 gene encodes two protein isoforms, TP53INP1 and TP53INP1, located into the nucleus. Their synthesis is increased during cellular stress by p53-mediated activation of transcription. Overexpression of these isoforms induces apoptosis, suggesting an involvement of TP53INP1s in p53-mediated cell death. It was recently shown that p53-dependent apoptosis is promoted by homeodomain-interacting protein kinase-2 (HIPK2), which is known to bind p53 and induce its phosphorylation in promyelocytic leukemia protein nuclear bodies (PML-NBs). In this work we show that TP53INP1s localize with p53, PML-IV, and HIPK2 into the PML-NBs. In addition, we show that TP53INP1s interact physically with HIPK2 and p53. In agreement with these results we demonstrate that TP53INP1s, in association with HIPK2, regulate p53 transcriptional activity on p21, mdm2, pig3, and bax promoters. Furthermore, TP53INP1s overexpression induces G₁ arrest and increases p53-mediated apoptosis. Although a TP53INP1s and HIPK2 additive effect was observed on apoptosis, G₁ arrest was weaker when HIPK2 was transfected together with TP53INP1. These results indicate that TP53INP1s and HIPK2 could be partners in regulating p53 activity.

Received for publication, February 25, 2003 , and in revised form, June 23, 2003.

^* This work was supported by grants from INSERM. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a predoctoral fellowship from the Ministère de la Recherche et de la Technologie.

^¶ Supported by a predoctoral fellowship from the Fondation pour la Recherche Médicale.

To whom correspondence should be addressed. Tel.: 33-491-827538; Fax: 33-491-826083; E-mail: dusetti{at}inserm-nacre.inserm-adr2.univ-mrs.fr.

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