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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11-12
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pubmed:dateCreated |
2008-6-23
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pubmed:abstractText |
Mitosis is a series of events leading to division of a cell by the process known as cytokinesis. Protein regulating cytokinesis 1 (PRC1) is a CDK substrate that associates with the mitotic spindle and functions in microtubule bundling. Previous studies revealed that loss of PRC1 is associated with chromosomal mis-segregation and atypical chromosome alignment. HSF2 is a DNA binding protein that we previously showed bookmarks the hsp70i gene during mitosis, an epigenetic mechanism which allows the hsp70i gene to re-establish transcriptional competence early in G1. Another study demonstrated that HSF2-/- mouse embryonic fibroblasts (MEFs) exhibit increased numbers of multinucleated cells vs. wild-type MEFs. This suggests that HSF2 is important for proper cytokinesis, but the mechanism was unknown. Here we report the existence of a direct interaction between HSF2 and PRC1. HSF2 and PRC1 associate during mitosis and co-localize during this phase of the cell cycle. PRC1 does not interact with the related protein HSF1, indicating the specificity of the HSF2-PRC1 interaction. Intriguingly, PRC1 is associated with the hsp70i promoter during mitosis. These results provide a potential mechanistic basis for the defective cytokinesis phenotype exhibited by HSF2-/- cells, as well as suggest a potential role for PRC1 in HSF2-mediated gene bookmarking.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/GM61053,
http://linkedlifedata.com/resource/pubmed/grant/GM64606,
http://linkedlifedata.com/resource/pubmed/grant/HD50043,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM061053-01A1,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM061053-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM061053-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM061053-04,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM064606-01A2,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM064606-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM064606-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM064606-04,
http://linkedlifedata.com/resource/pubmed/grant/T32 ES-07266
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-11278381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-11744923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-12082078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-12665592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-14754511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-15297875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-15326200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-15625105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-15662014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-16188444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-16603632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-17351640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-17512944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-17620410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-7553870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-7791788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-8529117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-9278053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-9619097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18570919-9885575
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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 |
Jul
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pubmed:issn |
1090-2422
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
314
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2224-30
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:18570919-Animals,
pubmed-meshheading:18570919-Cell Cycle Proteins,
pubmed-meshheading:18570919-HSP70 Heat-Shock Proteins,
pubmed-meshheading:18570919-HeLa Cells,
pubmed-meshheading:18570919-Heat-Shock Proteins,
pubmed-meshheading:18570919-Humans,
pubmed-meshheading:18570919-Jurkat Cells,
pubmed-meshheading:18570919-Mice,
pubmed-meshheading:18570919-Mitosis,
pubmed-meshheading:18570919-Promoter Regions, Genetic,
pubmed-meshheading:18570919-Recombinant Fusion Proteins,
pubmed-meshheading:18570919-Transcription Factors,
pubmed-meshheading:18570919-Two-Hybrid System Techniques
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pubmed:year |
2008
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pubmed:articleTitle |
PRC1 associates with the hsp70i promoter and interacts with HSF2 during mitosis.
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pubmed:affiliation |
Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY, 40536, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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