| Insights into the regulation of heat shock transcription factor 1 SUMO-1 modification. | |
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MedLine Citation:
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PMID: 12646186 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The transcriptional regulatory protein HSF1 is the key mediator of induced heat shock protein gene expression in response to elevated temperature and other stresses. Our previous studies identified stress-induced SUMO-1 modification of HSF1 as an important regulator of the DNA-binding activity of this factor. The underlying molecular mechanism by which stress leads to sumoylation of HSF1 was unknown. Prompted by previous studies indicating stress-induced phosphorylation at serine 307 of HSF1, a site very near the sumoylation site at lysine 298, we examined the role of this phosphorylation event in regulating SUMO-1 modification of HSF1. Using a combination of transfection and in vitro phosphorylation/sumoylation experiments, our results indicate that phosphorylation at serine 307 stimulates sumoylation of HSF1. Our results also reveal a role for a conserved leucine zipper sequence in the C-terminal region of HSF1 in inhibiting its SUMO-1 modification. Based on these data, we postulate that phosphorylation at serine 307 could stimulate HSF1 sumoylation by causing a conformation change that relieves the inhibitory effect of the C-terminal leucine zipper. |
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Authors:
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Roland S Hilgarth; Yiling Hong; Ok-Kyong Park-Sarge; Kevin D Sarge |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 303 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2003 Mar |
Date Detail:
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Created Date: 2003-03-20 Completed Date: 2003-05-22 Revised Date: 2011-11-02 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 196-200 Citation Subset: IM |
Affiliation:
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Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536-0298, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence DNA-Binding Proteins / chemistry, metabolism* Gene Expression Regulation* Glycogen Synthase Kinase 3 / metabolism Hela Cells Hot Temperature Humans Leucine / chemistry Lysine / chemistry Mitogen-Activated Protein Kinase 1 / metabolism Models, Genetic Molecular Sequence Data Mutagenesis, Site-Directed Mutation Phosphorylation Precipitin Tests Protein Biosynthesis Protein Structure, Tertiary SUMO-1 Protein / chemistry, metabolism* Serine / chemistry Temperature Transcription Factors Transfection |
| Grant Support | |
ID/Acronym/Agency:
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GM61053/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/DNA-Binding Proteins; 0/SUMO-1 Protein; 0/Transcription Factors; 0/heat shock transcription factor; 56-45-1/Serine; 56-87-1/Lysine; 61-90-5/Leucine; EC 2.7.11.1/glycogen synthase kinase 3 beta; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.11.26/Glycogen Synthase Kinase 3 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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