Document Detail


Insights into the regulation of heat shock transcription factor 1 SUMO-1 modification.
MedLine Citation:
PMID:  12646186     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Roland S Hilgarth; Yiling Hong; Ok-Kyong Park-Sarge; Kevin D Sarge
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  303     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2003 Mar 
Date Detail:
Created Date:  2003-03-20     Completed Date:  2003-05-22     Revised Date:  2011-11-02    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  196-200     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536-0298, USA.
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MeSH Terms
Descriptor/Qualifier:
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:
GM61053/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
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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