| Literature DB >> 17688198 |
Hongyan Xing1, Yiling Hong, Kevin D Sarge.
Abstract
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 (delta343-348)), 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.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17688198 PMCID: PMC1949333 DOI: 10.1379/csc-249r.1
Source DB: PubMed Journal: Cell Stress Chaperones ISSN: 1355-8145 Impact factor: 3.667