Insights into the regulation of heat shock transcription factor 1 SUMO-1 modification
| Autor: | Kevin D. Sarge, Roland S. Hilgarth, Ok Kyong Park-Sarge, Yiling Hong |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Leucine zipper
Hot Temperature Molecular Sequence Data SUMO-1 Protein Biophysics SUMO protein Biology Transfection environment and public health Biochemistry Serine Glycogen Synthase Kinase 3 Heat Shock Transcription Factors Leucine Heat shock protein Humans Amino Acid Sequence Phosphorylation HSF1 Molecular Biology Mitogen-Activated Protein Kinase 1 ATF3 Glycogen Synthase Kinase 3 beta Models Genetic Lysine fungi Temperature Cell Biology Precipitin Tests Protein Structure Tertiary Cell biology DNA-Binding Proteins Heat shock factor enzymes and coenzymes (carbohydrates) Gene Expression Regulation Protein Biosynthesis Mutation Mutagenesis Site-Directed HeLa Cells Transcription Factors |
| Zdroj: | Biochemical and Biophysical Research Communications. 303:196-200 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(03)00312-7 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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