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PMID: 15497499 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

On mechanisms that control heat shock transcription factor activity in metazoan cells.

Cell stress & chaperones ·Vol. 9 ·No. 2 ·2004-00-00 ·Pages 122-33

Voellmy R

Abstract

Heat shock factor Hsf in nonvertebrate animals and homologous heat shock factor Hsf1 in vertebrate animals are key transcriptional regulators of the stress protein response. Hsf/Hsf1 is constitutively present in cells but is, typically, only active during periods during which cells are experiencing a physical or chemical proteotoxic stress. It has become increasingly clear that regulation of Hsf/Hsf1 activity occurs at multiple levels: the oligomeric status of Hsf/Hsf1, its DNA-binding ability, posttranslational modification, transcriptional competence, nuclear/ subnuclear localization, as well as its interactions with regulatory cofactors or other transcription factors all appear to be carefully controlled. This review emphasizes work reported over the past several years suggesting that regulation at several of these levels is mediated by repressive interactions of Hsp90-containing multichaperone complexes and/or individual chaperones and Hsf/Hsf1.

MeSH Terms
Amino Acid Sequence Animals Base Sequence DNA-Binding Proteins/chemistry,metabolism Gene Expression Regulation HSP90 Heat-Shock Proteins/metabolism Heat Shock Transcription Factors Humans Models, Biological Protein Processing, Post-Translational Transcription Factors/genetics,metabolism Transcription, Genetic
Chemicals
DNA-Binding Proteins HSF1 protein, human HSP90 Heat-Shock Proteins Heat Shock Transcription Factors Transcription Factors
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Voellmy Richard
Department of Biochemistry and Molecular Biology, University of Miami, Gautier Building, Room 403, 1011 NW 15th Street, Miami, FL 33136, USA. [email protected]
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Article Info
Journal
Cell stress & chaperones
Abbr.
Cell Stress Chaperones
ISSN
1355-8145
Published
2004-00-00
Pages
122-33
Language
English
Region
Netherlands
NLM ID
9610925
PMCID
PMC1065292
Subset
IM
Grants
NIGMS NIH HHS · GM31125 · United States
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