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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2009-2-16
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pubmed:abstractText |
Acetylation of multiple lysine residues in the p53 plays critical roles in the protein stability and transcriptional activity of p53. To better understand how p53 acetylation is regulated, we generated a number of p53 mutants and examined acetylation of each mutant in transfected cells. We found that p53 mutants that are defective in tetramer formation are also defective in C-terminal lysine residue acetylation. Consistently, we found that several cancer-derived p53 mutants that bear mutations in the tetramerization domain cannot form oligomers and are defective in C-terminal lysine acetylation, and these mutants are inactive in p21 transactivation. We demonstrated that the acetyltransferase p300 interacts with and promotes acetylation of wild-type p53 but not with any of the artificially generated or human cancer-derived p53 mutants that are defective in oligomerization. These results, combined with a computer-aided crystal structure analysis, suggest a model in which p53 oligomerization precedes its acetylation by providing docking sites for acetyltransferases.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-10048932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-10075936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-10318779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-10473588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-11094089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-11099028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-11099047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-11250899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-11397945,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-11782467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-12944468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-14583457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-14982997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-15806143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-16916644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-17113101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-17189186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-17189187,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-17438265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-17965593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-18485870,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-7634336,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-9215639,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19106109-9891054
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5158-64
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pubmed:dateRevised |
2011-4-19
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pubmed:meshHeading |
pubmed-meshheading:19106109-Acetylation,
pubmed-meshheading:19106109-Cell Line, Tumor,
pubmed-meshheading:19106109-Crystallography, X-Ray,
pubmed-meshheading:19106109-Humans,
pubmed-meshheading:19106109-Models, Molecular,
pubmed-meshheading:19106109-Mutation,
pubmed-meshheading:19106109-Protein Stability,
pubmed-meshheading:19106109-Protein Structure, Quaternary,
pubmed-meshheading:19106109-Protein Structure, Tertiary,
pubmed-meshheading:19106109-Transcription Factors,
pubmed-meshheading:19106109-Tumor Suppressor Protein p53,
pubmed-meshheading:19106109-p300-CBP Transcription Factors
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pubmed:year |
2009
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pubmed:articleTitle |
p53 Oligomerization is essential for its C-terminal lysine acetylation.
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pubmed:affiliation |
Department of Radiation Oncology, University of North Carolina, Chapel Hill, North Carolina 27599-7512, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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