期刊
SCIENCE
卷 323, 期 5917, 页码 1063-1066出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1165946
关键词
-
资金
- NIH
- Turku Graduate School of Biomedical Sciences
- Academy of Finland
- Sigrid Juselius Foundation
- Abo Akademi University
- National Institute for General Medical Science
- National Institute for Aging
- Rice Institute for Biomedical Research
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据