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โœฆ   LIBER   โœฆ

Highlights: Volume 227, Number 1


Book ID
102882972
Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
504 KB
Volume
227
Category
Article
ISSN
0021-9541

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โœฆ Synopsis


Kim et al explore how HSF2 is regulated under conditions of cellular stress and how the interplay between HSF2 and HSF4a can regulate protein functions and play a role in activating target genes. The authors previously reported on the role of HSF4a on the regulation of HSF2. HSF2 levels are negatively correlated with HSF4a expression and the overexpression of HSF4a reduces hemin-induced HSF2 mRNA and protein levels. Immunoprecipitation assays showed that HSF2 binds to the oligomerization domain of HSF4a. Hemin treatment inhibited interaction and induced localization of HSF2 and HSF4a in the nucleus. In addition, hemin-induced HSP70 promoter activity was almost completely inhibited by HSF4a overexpression. These findings provide evidence that HSF2 is a specific target for HSF4a and suggest mechanisms for HSF2 regulation being controlled by HSF4a.


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