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Stress-Inducible Regulation of Heat Shock Factor 1 by the Deacetylase SIRT1
Abstract
Heat shock factor 1 (HSF1) is essential for protecting cells from protein-damaging stress associated with misfolded proteins and regulates the insulin-signaling pathway and aging. Here, we show that human HSF1 is inducibly acetylated at a critical residue that negatively regulates DNA binding activity. Activation of the deacetylase and longevity factor SIRT1 prolonged HSF1 binding to the heat shock promoter Hsp70 by maintaining HSF1 in a deacetylated, DNA–binding competent state. Conversely, down-regulation of SIRT1 accelerated the attenuation of the heat shock response (HSR) and release of HSF1 from its cognate promoter elements. These results provide a mechanistic basis for the requirement of HSF1 in the regulation of life span and establish a role for SIRT1 in protein homeostasis and the HSR.
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In mammalian cells, deacetylation of HSF-1 by SIRT1 potentiates the transactivation of heat-shock genes such as Hsp70, whereas down-regulation of SIRT1 attenuates the heat-shock response.
“In mammalian cells, deacetylation of HSF-1 by SIRT1 potentiates the transactivation of heat-shock genes such as Hsp70, whereas down-regulation of SIRT1 attenuates the heat-shock response (Westerheide et al., 2009).”
From The Hallmarks of Aging (2013) · cites this paper as Westerheide et al., 2009
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“For example, Sirtuin 1 (SIRT1) impacts the heat-shock response by deacetylating a lysine (K80) residue within the DNA binding domain (DBD) of heat shock factor 1 (HSF1)—acetylation of K80 blocks DNA binding (Westerheide et al., 2009).”
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Metadata
- Authors
- Westerheide, S. D., Anckar, J., Stevens, S. M., Sistonen, L., & Morimoto, R. I.
- Affiliations
- Department of Biochemistry, Molecular Biology and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL, 60208, USA.
- Venue
- Science
- Published
- 2009-02-20
- Volume
- 323
- Issue
- 5917
- Pages
- 1063-1066
- ISSN
- 0036-8075
- 1095-9203
- PMC
- PMC3429349
- Cited by
- 639
- References
- 6
- Language
- en
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