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. 2002 Jan;4(1):11-9.
doi: 10.1038/ncb714.

Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis

Gabriella D'Orazi  1 , Barbara Cecchinelli, Tiziana Bruno, Isabella Manni, Yuichiro Higashimoto, Shin'ichi Saito, Monica Gostissa, Sabrina Coen, Alessandra Marchetti, Giannino Del Sal, Guilia Piaggio, Maurizio Fanciulli, Ettore Appella, Silvia Soddu
Affiliations

Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis

Gabriella D'Orazi et al. Nat Cell Biol. 2002 Jan.

Abstract

Phosphorylation of p53 at Ser 46 was shown to regulate p53 apoptotic activity. Here we demonstrate that homeodomain-interacting protein kinase-2 (HIPK2), a member of a novel family of nuclear serine/threonine kinases, binds to and activates p53 by directly phosphorylating it at Ser 46. HIPK2 localizes with p53 and PML-3 into the nuclear bodies and is activated after irradiation with ultraviolet. Antisense inhibition of HIPK2 expression reduces the ultraviolet-induced apoptosis. Furthermore, HIPK2 and p53 cooperate in the activation of p53-dependent transcription and apoptotic pathways. These data define a new functional interaction between p53 and HIPK2 that results in the targeted subcellular localization of p53 and initiation of apoptosis.

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