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Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis.
- Source :
-
Nature Cell Biology . Jan2002, Vol. 4 Issue 1, p11. 9p. - Publication Year :
- 2002
-
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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PROTEIN kinases
*P53 antioncogene
*PHOSPHORYLATION
Subjects
Details
- Language :
- English
- ISSN :
- 14657392
- Volume :
- 4
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Nature Cell Biology
- Publication Type :
- Academic Journal
- Accession number :
- 8783636
- Full Text :
- https://doi.org/10.1038/ncb714