Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-1-7
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HIPK2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Hipk2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, Antisense, http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Pml protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1465-7392
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:11780126-Animals, pubmed-meshheading:11780126-Apoptosis, pubmed-meshheading:11780126-Carrier Proteins, pubmed-meshheading:11780126-Cell Nucleus, pubmed-meshheading:11780126-Enzyme Activation, pubmed-meshheading:11780126-Genes, Tumor Suppressor, pubmed-meshheading:11780126-Humans, pubmed-meshheading:11780126-Mice, pubmed-meshheading:11780126-Neoplasm Proteins, pubmed-meshheading:11780126-Nuclear Proteins, pubmed-meshheading:11780126-Oligonucleotides, Antisense, pubmed-meshheading:11780126-Phosphorylation, pubmed-meshheading:11780126-Protein Isoforms, pubmed-meshheading:11780126-Protein-Serine-Threonine Kinases, pubmed-meshheading:11780126-Serine, pubmed-meshheading:11780126-Transcription Factors, pubmed-meshheading:11780126-Transcriptional Activation, pubmed-meshheading:11780126-Tumor Cells, Cultured, pubmed-meshheading:11780126-Tumor Suppressor Protein p53, pubmed-meshheading:11780126-Tumor Suppressor Proteins, pubmed-meshheading:11780126-Ultraviolet Rays
pubmed:year
2002
pubmed:articleTitle
Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis.
pubmed:affiliation
Molecular Oncogenesis Laboratory, Regina Elena Cancer Institute, Via delle Messi d Oro 156, 00158 Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't