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Heat shock transcription factor HSF1 regulates the expression of the Huntingtin-interacting protein HYPK

The Huntingtin-interacting protein HYPK possesses chaperone-like activity. We hypothesized that the expression of HYPK could be regulated by heat shock factor HSF1, a transcriptional regulator of chaperone genes. HYPK expression in HeLa cells was assessed by RT-PCR and Western blot analysis. In vivo...

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Published in:Biochimica et biophysica acta 2014-03, Vol.1840 (3), p.1181-1187
Main Authors: Sakurai, Hiroshi, Sawai, Maki, Ishikawa, Yukio, Ota, Azumi, Kawahara, Ei
Format: Article
Language:English
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Summary:The Huntingtin-interacting protein HYPK possesses chaperone-like activity. We hypothesized that the expression of HYPK could be regulated by heat shock factor HSF1, a transcriptional regulator of chaperone genes. HYPK expression in HeLa cells was assessed by RT-PCR and Western blot analysis. In vivo binding of HSF1 to the HYPK promoter was analyzed by chromatin immunoprecipitation assays. The requirement for HYPK in heat-shocked cells was examined using HYPK-knockdown cells. Levels of HYPK mRNA were slightly increased by heat treatment; however, the levels decreased in HSF1-silenced cells. The HYPK promoter was bound by HSF1 in a heat-inducible manner; however, its core promoter activity was notably suppressed upon heat shock. When cells were exposed to heat shock, silencing HYPK caused a decrease in cell viability. HYPK is a novel target gene of HSF1. HSF1 maintains HYPK expression in heat-shocked cells. The maintenance of HYPK expression by HSF1 is necessary for the survival of cells under thermal stress conditions. •The HYPK protein possesses chaperone-like activity.•HSF1 is the master transcriptional activator of various chaperone genes.•The HYPK promoter is bound by HSF1 in a heat-inducible manner.•HSF1 maintains HYPK expression in heat-shocked cells.•HYPK expression is necessary for cell survival under thermal stress conditions.
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/j.bbagen.2013.12.006