RNA-mediated response to heat shock in mammalian cells

  title={RNA-mediated response to heat shock in mammalian cells},
  author={Ilya Shamovsky and Maxim V. Ivannikov and Eugene S. Kandel and David Gershon and Evgeny Nudler},
The heat-shock transcription factor 1 (HSF1) has an important role in the heat-shock response in vertebrates by inducing the expression of heat-shock proteins (HSPs) and other cytoprotective proteins. HSF1 is present in unstressed cells in an inactive monomeric form and becomes activated by heat and other stress stimuli. HSF1 activation involves trimerization and acquisition of a site-specific DNA-binding activity, which is negatively regulated by interaction with certain HSPs. Here we show… 

Isolation and characterization of the heat shock RNA 1.

It is shown that a large, noncoding RNA, HSR1, and the translation elongation factor eEF1A form a complex with HSF during HS and are required for its activation.

Signal Transduction Pathways Leading to Heat Shock Transcription.

HSP genes are regulated at the transcriptional level by heat shock transcription factor 1 (HSF1) that is activated by stress and binds to heat shock elements in HSP genes, and recent studies indicate important roles for histone modifications on H SP genes during heat shock.

Hsf1 and Hsp70 constitute a two-component feedback loop that regulates the yeast heat shock response

The results reveal the quantitative control mechanisms underlying the feedback loop charged with maintaining cytosolic proteostasis and uncovered a role for the N-terminal domain of Hsf1 in negatively regulating DNA binding.

Heat shock factor 1 promotes TERRA transcription and telomere protection upon heat stress

It is shown that telomere integrity is impacted by heat shock and that telomeric DNA damages are markedly enhanced in HSF1 deficient cells, and a new direct and essential function of HSF 1 is revealed in the transcriptional activation of TERRA and in telomeres protection upon stress.

Identification of Heat Shock Factor Binding Sites in the Drosophila Genome

Interestingly, the binding of HSF also coincides with puff regression at some sites, and two such sites contain the major developmentally regulated genes Eip74 and Eip75: key regulators in the response to 20-hydroxyecdysone, the main hormone responsible for the temporal coordination of post-embryonic development in Drosophila.

Heat shock factor 1 is a key regulator of the stress response in Chlamydomonas.

The characterization of heat shock factor 1 (HSF1), encoded by one of two HSF genes identified in the genome of Chlamydomonas reinhardtii, is reported here on, suggesting that HSF1 is a key regulator of the stress response in ChlamYDomonas.

Novel aspects of heat shock factors: DNA recognition, chromatin modulation and gene expression

This minireview focuses on the molecular mechanisms of DNA recognition, chromatin modulation and gene expression by yeast and mammalian HSFs.

Transformation of eEF1Bδ into heat‐shock response transcription factor by alternative splicing

The transcriptional role of eEF1BδL could provide new insights into the molecular mechanism of stress responses as well as help clarify the role of protein translation factors in stress responses.

Cell Division During Stress Proteostasis Network in T Cells Critical for Activation and Regulates a Major Activated as a Consequence of Lymphocyte Heat Shock Transcription Factor 1 Is

This study demonstrated that murine HSF1 became activated to the DNA-binding form and transactivated a large number of genes in lymphoid cells strictly as a consequence of receptor activation in the absence of apparent cellular stress, indicating thatHSF1 is critical for the cell cycle progression of lymphoid Cells activated under stressful conditions.

A transcription cofactor required for the heat‐shock response

The results indicate that Strap is an essential cofactor that acts at the level of chromatin control to regulate heat‐shock‐responsive transcription.



HSP90 Interacts with and Regulates the Activity of Heat Shock Factor 1 in Xenopus Oocytes

A new regulatory model is proposed in which HSP90 participates in modulating HSF1 at different points along the activation-deactivation pathway, influencing the interconversion between monomeric and trimeric conformations as well as transcriptional activation.

Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells.

Evidence is presented herein that 1) non-activated HSF1 forms a 1:1 complex with Hsp70, 2) both rates of heat-induced appearance ofHSF1 oligomers and rates of disappearance of HSF 1 heterodimers and monomers decrease when concentrations of unengaged Hsps are increased, and 3) transient overexpression of HSP70 inhibits heat activation of HSf1.

Activation of Heat Shock Gene Transcription by Heat Shock Factor 1 Involves Oligomerization, Acquisition of DNA-Binding Activity, and Nuclear Localization and Can Occur in the Absence of Stress

It is demonstrated that HSF1 can be activated in the absence of physiological stress and support is provided for a model of regulation ofHSF1 and HSF2 activity by a titratable negative regulatory factor.

The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression.

Hsp70 blocks the in vitro activation of HSF from its cryptic non-DNA-binding state to a DNA-binding form; this inhibitory effect of hsp70 is abolished by ATP.

Intramolecular Repression of Mouse Heat Shock Factor 1

It is shown that HSF1 behaves as a monomer which can be induced by increases in temperature to form active HSE-binding trimers and that mutations of either HR region cause activation in both systems.

Complex modes of heat shock factor activation

It appears that despite conservation of the HSE in evolution, the means by which HSF is activated to bind DNA in higher and lower eucaryotes may have diverged.

Multiple Components of the HSP90 Chaperone Complex Function in Regulation of Heat Shock Factor 1 In Vivo

The current evidence leads us to propose a model in which HSF1, HSP90 and p23 comprise a core heterocomplex required for rapid conformational switching through interaction with a dynamic series of HSP 90 subcomplexes.

Molecular chaperones as HSF1-specific transcriptional repressors.

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.

Multiple layers of regulation of human heat shock transcription factor 1

The existence of a fold-back structure that masks the transcription activation domain in the unstressed cell but is opened up by modification of hHSF1 and/or binding of a factor facilitating h HSF1 unfolding in the stressed cell is proposed.