Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6535
pubmed:dateCreated
1995-8-3
pubmed:abstractText
Central to the role of p53 in cell regulation are its sequence-specific interactions with genes that control the cell cycle and apoptosis. p53 response elements contain two or more copies of a somewhat promiscuous consensus sequence: 5'-XXXC(A,T)(T,A)GYY-3' (where X is a purine and Y is a pyrimidine) (ref. 3). The sequence-specific DNA-binding region of p53 resides in its central conserved region. Although this region itself is not known to be phosphorylated, the amino and carboxy termini of human p53 contain sites for phosphorylation by several protein kinases. We have examined the role of cyclin-dependent kinase (Cdk) shown previously to phosphorylate human p53 at serine 315 (ref. 5). We report here that p53 is efficiently and selectively phosphorylated by S and G2/M Cdks. Such phosphorylation markedly stimulates sequence-specific DNA binding by p53 and also causes a distinctive conformational change in p53 as revealed by partial protease analysis. Strikingly, Cdk phosphorylation also confers binding-site preference on p53. These data suggest a potential regulatory mechanism of p53 activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CDC2-CDC28 Kinases, http://linkedlifedata.com/resource/pubmed/chemical/CDK2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CDK4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 4, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
376
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
88-91
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7596441-Animals, pubmed-meshheading:7596441-Base Sequence, pubmed-meshheading:7596441-CDC2-CDC28 Kinases, pubmed-meshheading:7596441-Cell Line, pubmed-meshheading:7596441-Cyclin D1, pubmed-meshheading:7596441-Cyclin-Dependent Kinase 2, pubmed-meshheading:7596441-Cyclin-Dependent Kinase 4, pubmed-meshheading:7596441-Cyclin-Dependent Kinases, pubmed-meshheading:7596441-Cyclins, pubmed-meshheading:7596441-DNA, pubmed-meshheading:7596441-Humans, pubmed-meshheading:7596441-Molecular Sequence Data, pubmed-meshheading:7596441-Oligodeoxyribonucleotides, pubmed-meshheading:7596441-Oncogene Proteins, pubmed-meshheading:7596441-Phosphorylation, pubmed-meshheading:7596441-Protein Binding, pubmed-meshheading:7596441-Protein-Serine-Threonine Kinases, pubmed-meshheading:7596441-Proto-Oncogene Proteins, pubmed-meshheading:7596441-Retinoblastoma Protein, pubmed-meshheading:7596441-Spodoptera, pubmed-meshheading:7596441-Tumor Suppressor Protein p53
pubmed:year
1995
pubmed:articleTitle
Increased and altered DNA binding of human p53 by S and G2/M but not G1 cyclin-dependent kinases.
pubmed:affiliation
Department of Biological Sciences, Columbia University, New York, New York 10027, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.