NDLI: Homeodomain-interacting Protein Kinase-2 Stabilizes p27kip1 by Its Phosphorylation at Serine 10 and Contributes to Cell Motility*

Content Provider	PubMed Central
Author	Pierantoni, Giovanna Maria Esposito, Francesco Tornincasa, Mara Rinaldo, Cinzia Giuseppe, Viglietto Soddu, Silvia Fusco, Alfredo
Copyright Year	2011
Abstract	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.
Related Links	http://dx.doi.org/10.1074/jbc.M111.230854
Starting Page	29005
File Format	PDF
ISSN	1083351X
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	33
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-08-19
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Homeodomain-interacting Protein Kinase-2 Stabilizes p27kip1 by Its Phosphorylation at Serine 10 and Contributes to Cell Motility

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