Identification of the PP2A-interacting region of heat shock transcription factor 2

Hongyan Xing, Yiling Hong, Kevin D. Sarge

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Previous work in our laboratory demonstrated the existence of an association between heat shock transcription factor 2 (HSF2) and the serine/threonine phosphatase 2A, which is mediated by interaction between HSF2 and the A subunit (also called PR65) of this protein phosphatase. In light of the importance of HSF2-PP2A association for HSF2 cellular function, in this study, we have sought to dissect the sequences within HSF2 that are important for interaction with the A subunit of PP2A. The results of these experiments indicate that the HSF2 region comprising amino acids 343-363 is important for A subunit interaction. This region includes part of the C-terminal leucine zipper motif of HSF2 called heptad repeat C (HR-C). The results of transfection/ immunoprecipitation experiments also show that deletion of the 6 amino acids from 343 to 348 from HSF2 (HSF2 (Δ343-348)), is sufficient to prevent HSF2 from interacting with PP2A. These data provide insight into a new functional domain of HSF2, the PP2A A subunit-interacting region.

Original languageEnglish
Pages (from-to)192-197
Number of pages6
JournalCell Stress and Chaperones
Issue number2
StatePublished - Jun 2007

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology


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