scholarly journals Interplay between mammalian heat shock factors 1 and 2 in physiology and pathology

FEBS Journal ◽  
2021 ◽  
Author(s):  
Pia Roos‐Mattjus ◽  
Lea Sistonen
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

Regulation of loquat fruit low temperature response and lignification involves interaction of heat shock factors and genes associated with lignin biosynthesis

2016 ◽  
Vol 39 (8) ◽  
pp. 1780-1789 ◽  
Author(s):  
Jiao-ke Zeng ◽  
Xian Li ◽  
Jing Zhang ◽  
Hang Ge ◽  
Xue-ren Yin ◽  
...  
Keyword(s):  
Heat Shock ◽  
Low Temperature ◽  
Temperature Response ◽  
Lignin Biosynthesis ◽  
Heat Shock Factors

scholarly journals Heat shock factor 2 is required for maintaining proteostasis against febrile-range thermal stress and polyglutamine aggregation

2011 ◽  
Vol 22 (19) ◽  
pp. 3571-3583 ◽  
Author(s):  
Toyohide Shinkawa ◽  
Ke Tan ◽  
Mitsuaki Fujimoto ◽  
Naoki Hayashida ◽  
Kaoru Yamamoto ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Protein Misfolding ◽  
Reproductive Organs ◽  
Heat Shock Factors ◽  
Mild Heat ◽  
Promising Therapeutic Target ◽  
Αb Crystallin ◽  
Shock Proteins ◽  
Polyglutamine Protein

Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs. However, the fundamental roles of HSF2 in vertebrate cells have not been identified. Here we find that vertebrate HSF2 is activated during heat shock in the physiological range. HSF2 deficiency reduces threshold for chicken HSF3 or mouse HSF1 activation, resulting in increased HSP expression during mild heat shock. HSF2-null cells are more sensitive to sustained mild heat shock than wild-type cells, associated with the accumulation of ubiquitylated misfolded proteins. Furthermore, loss of HSF2 function increases the accumulation of aggregated polyglutamine protein and shortens the lifespan of R6/2 Huntington's disease mice, partly through αB-crystallin expression. These results identify HSF2 as a major regulator of proteostasis capacity against febrile-range thermal stress and suggest that HSF2 could be a promising therapeutic target for protein-misfolding diseases.

scholarly journals Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability.

1991 ◽  
Vol 5 (10) ◽  
pp. 1902-1911 ◽  
Author(s):  
K D Sarge ◽  
V Zimarino ◽  
K Holm ◽  
C Wu ◽  
R I Morimoto
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Heat Shock Factors ◽  
Binding Ability

scholarly journals HSFs drive stress type-specific transcription of genes and enhancers

2021 ◽  
Author(s):  
Samu V Himanen ◽  
Mikael C Puustinen ◽  
Alejandro J Da Silva ◽  
Anniina Vihervaara ◽  
Lea Sistonen
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Rna Polymerase Ii ◽  
Molecular Mechanisms ◽  
Gene Promoters ◽  
Heat Shock Factors ◽  
Pol Ii ◽  
Bona Fide ◽  
Stressed Cells ◽  
First Time

Reprogramming of transcription is critical for the survival under cellular stress. Heat shock has provided an excellent model to investigate nascent transcription in stressed cells, but the molecular mechanisms orchestrating RNA synthesis during other types of stress are unknown. We utilized PRO-seq and ChIP-seq to study how Heat Shock Factors, HSF1 and HSF2, coordinate transcription at genes and enhancers upon oxidative stress and heat shock. We show that pause-release of RNA polymerase II (Pol II) is a universal mechanism regulating gene transcription in stressed cells, while enhancers are activated at the level of Pol II recruitment. Moreover, besides functioning as conventional promoter-binding transcription factors, HSF1 and HSF2 bind to stress-induced enhancers to trigger Pol II pause-release from poised gene promoters. Importantly, HSFs act at distinct genes and enhancers in a stress type-specific manner. HSF1 binds to many chaperone genes upon oxidative and heat stress but activates them only in heat-shocked cells. Under oxidative stress, HSF1 and HSF2 trans-activate genes independently of each other, demonstrating, for the first time, that HSF2 is a bona fide transcription factor. Taken together, we show that HSFs function as multi-stress-responsive factors that activate specific genes and enhancers when encountering changes in temperature and redox state.

scholarly journals The “HSF connection”: Pleiotropic regulation and activities of Heat Shock Factors shape pathophysiological brain development

2020 ◽  
Vol 725 ◽  
pp. 134895
Author(s):  
Agathe Duchateau ◽  
Aurélie de Thonel ◽  
Rachid El Fatimy ◽  
Véronique Dubreuil ◽  
Valérie Mezger
Keyword(s):  
Heat Shock ◽  
Brain Development ◽  
Heat Shock Factors

scholarly journals Molecular Mechanisms of Heat Shock Factors in Cancer

Cells ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 1202
Author(s):  
Mikael Christer Puustinen ◽  
Lea Sistonen
Keyword(s):  
Heat Shock ◽  
Molecular Mechanisms ◽  
Expression Patterns ◽  
Heat Shock Factors ◽  
Therapeutic Approaches ◽  
The Past ◽  
Cancer Types ◽  
Cellular Pathways ◽  
As Stress ◽  
Regulatory Functions

Malignant transformation is accompanied by alterations in the key cellular pathways that regulate development, metabolism, proliferation and motility as well as stress resilience. The members of the transcription factor family, called heat shock factors (HSFs), have been shown to play important roles in all of these biological processes, and in the past decade it has become evident that their activities are rewired during tumorigenesis. This review focuses on the expression patterns and functions of HSF1, HSF2, and HSF4 in specific cancer types, highlighting the mechanisms by which the regulatory functions of these transcription factors are modulated. Recently developed therapeutic approaches that target HSFs are also discussed.

Role of Heat Shock Factors in Diseases and Immunity

2020 ◽  
Author(s):  
Boopathi Balasubramaniam ◽  
Krishnaswamy Balamurugan
Keyword(s):  
Heat Shock ◽  
Heat Shock Factors

Heat shock factors in carrot: genome-wide identification, classification, and expression profiles response to abiotic stress

2014 ◽  
Vol 42 (5) ◽  
pp. 893-905 ◽  
Author(s):  
Ying Huang ◽  
Meng-Yao Li ◽  
Feng Wang ◽  
Zhi-Sheng Xu ◽  
Wei Huang ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Heat Shock ◽  
Expression Profiles ◽  
Heat Shock Factors ◽  
Genome Wide

scholarly journals The mitogen-activated protein kinase 4-phosphorylated heat shock factor A4A regulates responses to combined salt and heat stresses

2019 ◽  
Vol 70 (18) ◽  
pp. 4903-4918 ◽  
Author(s):  
Norbert Andrási ◽  
Gábor Rigó ◽  
Laura Zsigmond ◽  
Imma Pérez-Salamó ◽  
Csaba Papdi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Map Kinases ◽  
Target Genes ◽  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
Phosphorylation Site ◽  
Heat Shock Factor ◽  
Mitogen Activated Protein Kinase ◽  
Heat Shock Factors ◽  
Mitogen Activated Protein

Abstract Heat shock factors regulate responses to high temperature, salinity, water deprivation, or heavy metals. Their function in combinations of stresses is, however, not known. Arabidopsis HEAT SHOCK FACTOR A4A (HSFA4A) was previously reported to regulate responses to salt and oxidative stresses. Here we show, that the HSFA4A gene is induced by salt, elevated temperature, and a combination of these conditions. Fast translocation of HSFA4A tagged with yellow fluorescent protein from cytosol to nuclei takes place in salt-treated cells. HSFA4A can be phosphorylated not only by mitogen-activated protein (MAP) kinases MPK3 and MPK6 but also by MPK4, and Ser309 is the dominant MAP kinase phosphorylation site. In vivo data suggest that HSFA4A can be the substrate of other kinases as well. Changing Ser309 to Asp or Ala alters intramolecular multimerization. Chromatin immunoprecipitation assays confirmed binding of HSFA4A to promoters of target genes encoding the small heat shock protein HSP17.6A and transcription factors WRKY30 and ZAT12. HSFA4A overexpression enhanced tolerance to individually and simultaneously applied heat and salt stresses through reduction of oxidative damage. Our results suggest that this heat shock factor is a component of a complex stress regulatory pathway, connecting upstream signals mediated by MAP kinases MPK3/6 and MPK4 with transcription regulation of a set of stress-induced target genes.

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