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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1993-6-29
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pubmed:abstractText |
Overexpression of wild-type p53 prevents cells from entering the S phase of the cell cycle. The amino-terminal transactivation region of p53 is phosphorylated by several protein kinases, including DNA-PK, a nuclear serine/threonine protein kinase that in vitro requires DNA for activity. DNA-PK was recently shown to phosphorylate serines 15 and 37 of human p53 (Lees-Miller et al., 1992. Mol. Cell. Biol., 12, 5041-5049). To prevent phosphorylation at these sites, mutants were constructed that changed the codons for serine 15 or serine 37 to alanine codons. Expression of p53-Ala-37 in stably transformed T98G cells blocked progression of the cells into S phase as well as did the expression of wild-type p53. In contrast, p53-Ala-15 was partially defective in blocking cell cycle progression. Several cell clones transformed with the mutant p53-Ala-15 gene expressed normal levels of p53 mRNA but accumulated little or no detectable p53 protein. However, by using a transient expression system driven by a strong cytomegalovirus promoter, we showed that the inability of p53-Ala-15 to fully block cell cycle progression was not due to inadequate levels of expression or to a failure of the mutant protein to accumulate in the nucleus. These results suggest that phosphorylation of Ser-15 may affect p53 function.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:geneSymbol |
p53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1519-28
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8502477-Amino Acid Sequence,
pubmed-meshheading:8502477-Antibodies, Monoclonal,
pubmed-meshheading:8502477-Base Sequence,
pubmed-meshheading:8502477-Blotting, Northern,
pubmed-meshheading:8502477-Cell Cycle,
pubmed-meshheading:8502477-Cell Line,
pubmed-meshheading:8502477-Genes, p53,
pubmed-meshheading:8502477-Humans,
pubmed-meshheading:8502477-Immunoblotting,
pubmed-meshheading:8502477-Kinetics,
pubmed-meshheading:8502477-Molecular Sequence Data,
pubmed-meshheading:8502477-Mutagenesis, Site-Directed,
pubmed-meshheading:8502477-Oligodeoxyribonucleotides,
pubmed-meshheading:8502477-Peptides,
pubmed-meshheading:8502477-Phosphorylation,
pubmed-meshheading:8502477-Polymerase Chain Reaction,
pubmed-meshheading:8502477-Protein Kinases,
pubmed-meshheading:8502477-RNA, Messenger,
pubmed-meshheading:8502477-Serine,
pubmed-meshheading:8502477-Transfection,
pubmed-meshheading:8502477-Tumor Suppressor Protein p53
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pubmed:year |
1993
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pubmed:articleTitle |
Mutation of the serine 15 phosphorylation site of human p53 reduces the ability of p53 to inhibit cell cycle progression.
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pubmed:affiliation |
Laboratory of Cell Biology, National Institutes of Health, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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