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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2005-3-28
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pubmed:abstractText |
Heat shock transcription factor 1 (HSF1) is activated by pathophysiologic stresses and activation leads to an increased cellular level of heat shock proteins (Hsp(s)). Although the activation of HSF1 occurs via multiple stress-induced processes such as hyperphosphorylation, the exact cellular mechanism of HSF1 activation is still unclear. Here we show polo-like kinase 1 (PLK1) and HSF1 interact in vivo using the tandem affinity purification system. Although the interaction between HSF1 and PLK1 is increased by thermal stress, overexpression of PLK1 did not affect HSF1 trimerization or DNA binding activity. This interaction results in the phosphorylation of HSF1 on serine 419 by PLK1. Interestingly, mutation of serine 419 to alanine inhibited heat-stress induced HSF1 nuclear translocation. Our results suggest that the phosphorylation of HSF1 by PLK1 is an essential step for HSF1 nuclear translocation by heat stress.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
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/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/heat shock transcription factor,
http://linkedlifedata.com/resource/pubmed/chemical/polo-like kinase 1
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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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 |
1
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12653-7
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:15661742-Active Transport, Cell Nucleus,
pubmed-meshheading:15661742-Cell Cycle Proteins,
pubmed-meshheading:15661742-Cell Line,
pubmed-meshheading:15661742-Cross-Linking Reagents,
pubmed-meshheading:15661742-DNA,
pubmed-meshheading:15661742-DNA, Complementary,
pubmed-meshheading:15661742-DNA-Binding Proteins,
pubmed-meshheading:15661742-Dimerization,
pubmed-meshheading:15661742-Genetic Vectors,
pubmed-meshheading:15661742-Green Fluorescent Proteins,
pubmed-meshheading:15661742-Hot Temperature,
pubmed-meshheading:15661742-Humans,
pubmed-meshheading:15661742-Immunoblotting,
pubmed-meshheading:15661742-Microscopy, Fluorescence,
pubmed-meshheading:15661742-Phosphorylation,
pubmed-meshheading:15661742-Plasmids,
pubmed-meshheading:15661742-Protein Binding,
pubmed-meshheading:15661742-Protein Kinases,
pubmed-meshheading:15661742-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15661742-Proto-Oncogene Proteins,
pubmed-meshheading:15661742-Serine,
pubmed-meshheading:15661742-Time Factors,
pubmed-meshheading:15661742-Transcription Factors,
pubmed-meshheading:15661742-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and mediates its nuclear translocation during heat stress.
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pubmed:affiliation |
Oral Biology Research Institute, Chosun University College of Dentistry, Gwangju 501-759, Korea.
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pubmed:publicationType |
Journal Article
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