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  Interplay of Acetyltransferase EP300 and the Proteasome System in Regulating Heat Shock Transcription Factor 1

Raychaudhuri, S., Loew, C., Körner, R., Pinkert, S., Theis, M., Hayer-Hartl, M., et al. (2014). Interplay of Acetyltransferase EP300 and the Proteasome System in Regulating Heat Shock Transcription Factor 1. CELL, 156(5), 975-985. doi:10.1016/j.cell.2014.01.055.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-F04A-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-F04C-C
Genre: Journal Article

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 Creators:
Raychaudhuri, Swasti1, Author              
Loew, Christian1, Author              
Körner, Roman1, Author              
Pinkert, Stefan1, Author              
Theis, Mirko2, Author
Hayer-Hartl, Manajit3, Author              
Buchholz, Frank2, Author
Hartl, F. Ulrich1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2external, ou_persistent22              
3Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: MOLECULAR CHAPERONES; CAENORHABDITIS-ELEGANS; PROTEIN STABILITY; IN-VIVO; STRESS; PROTEOSTASIS; ACTIVATION; GENE; HSF1; LOCALIZATION
 Abstract: When exposed to proteotoxic environmental conditions, mammalian cells activate the cytosolic stress response in order to restore protein homeostasis. A key feature of this response is the heat shock transcription factor 1 (HSF1)-dependent expression of molecular chaperones. Here, we describe the results of an RNA interference screen in HeLa cells to identify modulators of stress response induction and attenuation. The modulator proteins are localized in multiple cellular compartments, with chromatin modifiers and nuclear protein quality control playing a central regulatory role. We find that the acetyltransferase, EP300, controls the cellular level of activatable HSF1. This involves acetylation of HSF1 at multiple lysines not required for function and results in stabilization of HSF1 against proteasomal turnover. Acetylation of functionally critical lysines during stress serves to fine-tune HSF1 activation. Finally, the nuclear proteasome system functions in attenuating the stress response by degrading activated HSF1 in a manner linked with the clearance of misfolded proteins.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: CELL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 156 (5) Sequence Number: - Start / End Page: 975 - 985 Identifier: ISSN: 0092-8674