Insights into the regulation of heat shock transcription factor 1 SUMO-1 modification

被引:35
作者
Hilgarth, RS
Hong, YL
Park-Sarge, OK
Sarge, KD [1 ]
机构
[1] Univ Kentucky, Albert B Chandler Med Ctr, Dept Mol & Cellular Biochem, Lexington, KY 40536 USA
[2] Univ Kentucky, Albert B Chandler Med Ctr, Dept Physiol, Lexington, KY 40536 USA
[3] Univ Cincinnati, Coll Med, Dept Cell Biol Neurobiol & Anat, Cincinnati, OH 45267 USA
关键词
sumoylation; HSFI; phosphorylation;
D O I
10.1016/S0006-291X(03)00312-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:196 / 200
页数:5
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