The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Molecularchaperones as HSF1-specific transcriptional repressors
Open accessAbstract
The rapid yet transient transcriptional activation of heat shock genes is mediated by the reversible conversion of HSF1 from an inert negatively regulated monomer to a transcriptionally active DNA-binding trimer. During attenuation of the heat shock response, transcription of heat shock genes returns to basal levels and HSF1 reverts to an inert monomer. These events coincide with elevated levels of Hsp70 and other heat shock proteins (molecular chaperones). Here, we show that the molecular chaperone Hsp70 and the cochaperone Hdj1 interact directly with the transactivation domain of HSF1 and repress heat shock gene transcription. Overexpression of either chaperone represses the transcriptional activity of a transfected GAL4-HSF1 activation domain fusion protein and endogenous HSF1. As neither the activation of HSF1 DNA binding nor inducible phosphorylation of HSF1 was affected, the primary autoregulatory role of Hsp70 is to negatively regulate HSF1 transcriptional activity. These results reveal that the repression of heat shock gene transcription, which occurs during attenuation, is due to the association of Hsp70 with the HSF1 transactivation domain, thus providing a plausible explanation for the role of molecular chaperones in at least one key step in the autoregulation of the heat shock response.
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Citations
Cites
Transcriptional Activation by Tetracyclines in Mammalian Cells
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Speculations on the functions of the major heat shock and glucose-regulated proteins
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Cells in Stress: Transcriptional Activation of Heat Shock Genes
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Self-citationInteraction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and Assembly
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Heat Shock Transcription Factors: Structure and Regulation
Wu, C. (1995) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cb.11.110195.002301 · Cited by 1,231 · cited 2×
“Upon exposure of cells to seemingly diverse stress conditions, HSFs become activated to a DNA-binding, transcriptionally active state, which results in the preferential transcription of heat shock genes (Mosser et al. 1988; Morimoto et al. 1990; Lis and Wu 1993; Morimoto 1993; Rabindran et al. 1993; Sarge et al. 1993;…”
BackgroundRole of the Human Heat Shock Protein hsp70 in Protection against Stress-Induced Apoptosis
Mosser, D. D., Caron, A. W., Bourget, L., Denis-Larose, C., & Massie, B. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5317 · Cited by 952
Self-citationRegulation of the specific DNA binding function of p53
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Self-citationPeptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly
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Cited by
Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,906
Self-citationThe Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Self-citationHeat shock factors: integrators of cell stress, development and lifespan
Åkerfelt, M., Morimoto, R. I., & Sistonen, L. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2938 · Cited by 1,455
Self-citationCellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 991
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872
Self-citation
Metadata
- Authors
- Shi, Y., Mosser, D. D., & Morimoto, R. I.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1998-03-01
- Volume
- 12
- Issue
- 5
- Pages
- 654-666
- ISSN
- 0890-9369 (ISSN-L)
- OpenAlex
- W2152622809
- Cited by
- 655
- References
- 60
- Type
- posted content
- Language
- en
- Open access
- diamond
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