ATF1 Modulates the Heat Shock Response by Regulating the Stress-Inducible Heat Shock Factor 1 Transcription Complex

The heat shock response is an evolutionally conserved adaptive response to high temperatures that controls proteostasis capacity and is regulated mainly by an ancient heat shock factor (HSF). However, the regulation of target genes by the stress-inducible HSF1 transcription complex has not yet been...

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Bibliographic Details
Published in:Molecular and cellular biology 2015-01, Vol.35 (1), p.11-25
Main Authors: Takii, Ryosuke, Fujimoto, Mitsuaki, Tan, Ke, Takaki, Eiichi, Hayashida, Naoki, Nakato, Ryuichiro, Shirahige, Katsuhiko, Nakai, Akira
Format: Article
Language:English
Subjects:
Activating Transcription Factor 1 - metabolism
Animals
Cells, Cultured
Chromatin - metabolism
CREB-Binding Protein - metabolism
DNA Helicases - metabolism
DNA-Binding Proteins - metabolism
Fibroblasts - metabolism
Gene Expression Regulation
Heat Shock Transcription Factors
Heat-Shock Proteins - metabolism
Heat-Shock Response
Hot Temperature
Mice
Nuclear Proteins - metabolism
Phosphorylation
Promoter Regions, Genetic
Protein Binding
RNA Interference
Transcription Factors - metabolism
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Summary:The heat shock response is an evolutionally conserved adaptive response to high temperatures that controls proteostasis capacity and is regulated mainly by an ancient heat shock factor (HSF). However, the regulation of target genes by the stress-inducible HSF1 transcription complex has not yet been examined in detail in mammalian cells. In the present study, we demonstrated that HSF1 interacted with members of the ATF1/CREB family involved in metabolic homeostasis and recruited them on the HSP70 promoter in response to heat shock. The HSF1 transcription complex, including the chromatin-remodeling factor BRG1 and lysine acetyltransferases p300 and CREB-binding protein (CBP), was formed in a manner that was dependent on the phosphorylation of ATF1. ATF1-BRG1 promoted the establishment of an active chromatin state and HSP70 expression during heat shock, whereas ATF1-p300/CBP accelerated the shutdown of HSF1 DNA-binding activity during recovery from acute stress, possibly through the acetylation of HSF1. Furthermore, ATF1 markedly affected the resistance to heat shock. These results revealed the unanticipated complexity of the primitive heat shock response mechanism, which is connected to metabolic adaptation.
ISSN:1098-5549
0270-7306
1098-5549
DOI:10.1128/MCB.00754-14