Homeodomain-interacting protein kinase-2 stabilizes p27 kip1 by its phosphorylation at serine 10 and contributes to cell motility

Giovanna Maria Pierantoni, Francesco Esposito, Mara Tornincasa, Cinzia Rinaldo, Giuseppe Viglietto, Silvia Soddu, Alfredo Fusco

Research output: Contribution to journalArticlepeer-review


HIPK2 is a serine/threonine kinase that acts as a coregulator of an increasing number of factors involved in cell survival and proliferation during development and in response to different types of stress. Here we report on a novel target of HIPK2, the cyclin-dependent kinase inhibitor p27kip1. HIPK2 phosphorylates p27kip1 in vitro and in vivo at serine 10, an event that accounts for 80% of the total p27kip1 phosphorylation and plays a crucial role in the stability of the protein. Indeed, HIPK2 depletion by transient or stable RNA interference in tumor cells of different origin was consistently associated with strong reduction of p27kip1 phosphorylation at serine 10 and of p27kip1 stability. An initial evaluation of the functional relevance of this HIPK2-mediated regulation of p27kip1 revealed a contribution to cell motility, rather than to cell proliferation, but only in cells that do not express wild-type p53.

Original languageEnglish
Pages (from-to)29005-29013
Number of pages9
JournalJournal of Biological Chemistry
Issue number33
Publication statusPublished - Aug 19 2011

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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