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

Roland S. Hilgarth, Yiling Hong, Ok Kyong Park-Sarge, Kevin D. Sarge

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


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.

Original languageEnglish
Pages (from-to)196-200
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Mar 28 2003

Bibliographical note

Funding Information:
This work was supported by NIH Grant GM61053 and ACS Grant RPG-98525. We gratefully acknowledge Mike Matunis for generously providing SUMO-1 antibodies, and also thank other members of our laboratory for helpful discussions.


  • HSF1
  • Phosphorylation
  • Sumoylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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