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Updated: May 4, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
Heat shock transcription factor HSF1 regulates the expression of the Huntingtin-interacting protein HYPK
Hiroshi Sakurai1, Maki Sawai1, Yukio Ishikawa1
1Division of Health Sciences, Kanazawa University Graduate School of Medical Science, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan.
Background:
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.
Methods:
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.
Results:
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.
Conclusions:
HYPK is a novel target gene of HSF1. HSF1 maintains HYPK expression in heat-shocked cells.
General Significance:
The maintenance of HYPK expression by HSF1 is necessary for the survival of cells under thermal stress conditions.
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