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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1997-4-24
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pubmed:abstractText |
Heat shock transcription factor 1 (HSF1) is constitutively expressed in mammalian cells and negatively regulated for DNA binding and transcriptional activity. Upon exposure to heat shock and other forms of chemical and physiological stress, these activities of HSF1 are rapidly induced. In this report, we demonstrate that constitutive phosphorylation of HSF1 at serine residues distal to the transcriptional activation domain functions to repress transactivation. Tryptic phosphopeptide analysis of a collection of chimeric GAL4-HSF1 deletion and point mutants identified a region of constitutive phosphorylation encompassing serine residues 303 and 307. The significance of phosphorylation at serines 303 and 307 in the regulation of HSF1 transcriptional activity was demonstrated by transient transfection and assay of a chloramphenicol acetyltransferase reporter construct. Whereas the transfected wild-type GAL4-HSF1 chimera is repressed for transcriptional activity and derepressed by heat shock, mutation of serines 303 and 307 to alanine results in derepression to a high level of constitutive activity. Similar results were obtained with mutation of these serine residues in the context of full-length HSF1. These data reveal that constitutive phosphorylation of serines 303 and 307 has an important role in the negative regulation of HSF1 transcriptional activity at control temperatures.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-14732014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-1546322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-1643656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-1871105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-1936996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-1943760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-2257625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-2686840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-2858050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-3044613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-3211126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-3419505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-6865942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7585624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7592665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7593328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7623825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7623826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7628692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7638169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7760831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7780739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7917334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7935471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-7958915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8013461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8134388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8334697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8389721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8421783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8441385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8451637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8455593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8455624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8497256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8497261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8497263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8526841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8588977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8622685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8631933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8689565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8940068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9121459-8946918
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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 |
Apr
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2107-15
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9121459-Humans,
pubmed-meshheading:9121459-Animals,
pubmed-meshheading:9121459-Mice,
pubmed-meshheading:9121459-Serine,
pubmed-meshheading:9121459-Temperature,
pubmed-meshheading:9121459-Phosphorylation,
pubmed-meshheading:9121459-DNA,
pubmed-meshheading:9121459-Amino Acid Sequence,
pubmed-meshheading:9121459-HeLa Cells,
pubmed-meshheading:9121459-Binding Sites,
pubmed-meshheading:9121459-Molecular Sequence Data,
pubmed-meshheading:9121459-Peptide Mapping,
pubmed-meshheading:9121459-3T3 Cells,
pubmed-meshheading:9121459-DNA-Binding Proteins,
pubmed-meshheading:9121459-Transfection,
pubmed-meshheading:9121459-Sequence Deletion,
pubmed-meshheading:9121459-Transcriptional Activation,
pubmed-meshheading:9121459-Transcription Factors,
pubmed-meshheading:9121459-Heat-Shock Proteins,
pubmed-meshheading:9121459-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9121459-COS Cells,
pubmed-meshheading:9121459-Point Mutation
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