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      HSF1Base: A Comprehensive Database of HSF1 (Heat Shock Factor 1) Target Genes

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          Abstract

          HSF1 (heat shock factor 1) is an evolutionarily conserved master transcriptional regulator of the heat shock response (HSR) in eukaryotic cells. In response to high temperatures, HSF1 upregulates genes encoding molecular chaperones, also called heat shock proteins, which assist the refolding or degradation of damaged intracellular proteins. Accumulating evidence reveals however that HSF1 participates in several other physiological and pathological processes such as differentiation, immune response, and multidrug resistance, as well as in ageing, neurodegenerative demise, and cancer. To address how HSF1 controls these processes one should systematically analyze its target genes. Here we present a novel database called HSF1Base (hsf1base.org) that contains a nearly comprehensive list of HSF1 target genes identified so far. The list was obtained by manually curating publications on individual HSF1 targets and analyzing relevant high throughput transcriptomic and chromatin immunoprecipitation data derived from the literature and the Yeastract database. To support the biological relevance of HSF1 targets identified by high throughput methods, we performed an enrichment analysis of (potential) HSF1 targets across different tissues/cell types and organisms. We found that general HSF1 functions (targets are expressed in all tissues/cell types) are mostly related to cellular proteostasis. Furthermore, HSF1 targets that are conserved across various animal taxa operate mostly in cellular stress pathways (e.g., autophagy), chromatin remodeling, ribosome biogenesis, and ageing. Together, these data highlight diverse roles for HSF1, expanding far beyond the HSR.

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          Most cited references70

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          The heat shock response: life on the verge of death.

          Organisms must survive a variety of stressful conditions, including sudden temperature increases that damage important cellular structures and interfere with essential functions. In response to heat stress, cells activate an ancient signaling pathway leading to the transient expression of heat shock or heat stress proteins (Hsps). Hsps exhibit sophisticated protection mechanisms, and the most conserved Hsps are molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. In this Review, we summarize the concepts of the protective Hsp network. Copyright © 2010 Elsevier Inc. All rights reserved.
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            Regulation of aging and age-related disease by DAF-16 and heat-shock factor.

            A.-L. Hsu (2003)
            The Caenorhabditis elegans transcription factor HSF-1, which regulates the heat-shock response, also influences aging. Reducing hsf-1 activity accelerates tissue aging and shortens life-span, and we show that hsf-1 overexpression extends lifespan. We find that HSF-1, like the transcription factor DAF-16, is required for daf-2-insulin/IGF-1 receptor mutations to extend life-span. Our findings suggest this is because HSF-1 and DAF-16 together activate expression of specific genes, including genes encoding small heat-shock proteins, which in turn promote longevity. The small heat-shock proteins also delay the onset of polyglutamine-expansion protein aggregation, suggesting that these proteins couple the normal aging process to this type of age-related disease.
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              Heat shock factors: integrators of cell stress, development and lifespan.

              Heat shock factors (HSFs) are essential for all organisms to survive exposures to acute stress. They are best known as inducible transcriptional regulators of genes encoding molecular chaperones and other stress proteins. Four members of the HSF family are also important for normal development and lifespan-enhancing pathways, and the repertoire of HSF targets has thus expanded well beyond the heat shock genes. These unexpected observations have uncovered complex layers of post-translational regulation of HSFs that integrate the metabolic state of the cell with stress biology, and in doing so control fundamental aspects of the health of the proteome and ageing.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                19 November 2019
                November 2019
                : 20
                : 22
                : 5815
                Affiliations
                [1 ]Department of Genetics, Institute of Biology, Eötvös Loránd University, Pázmány Péter stny. 1/C, H-1117 Budapest, Hungary; d.kowacs@ 123456gmail.com (D.K.); tsigmond@ 123456gmail.com (T.S.); bernadette.hotzi@ 123456ttk.elte.hu (B.H.); bbazsi41@ 123456caesar.elte.hu (B.B.); fazekasda@ 123456gmail.com (D.F.)
                [2 ]Earlham Institute, Norwich NR4 7UZ, UK
                [3 ]Quadram Institute, Norwich NR4 7UA, UK
                [4 ]Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, University of Technology, H-1111 Budapest, Hungary; deak@ 123456mail.bme.hu
                [5 ]MTA-ELTE Genetics Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary
                Author notes
                [* ]Correspondence: vellai@ 123456falco.elte.hu (T.V.); barna.janos@ 123456ttk.elte.hu (J.B.); Tel.: +36-1-372-2500 (ext. 8684) (T.V.); +36-1-372-2500 (ext. 8349) (J.B.); Fax: +36-1-372-2641 (T.V.)
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0002-9242-0939
                Article
                ijms-20-05815
                10.3390/ijms20225815
                6888953
                31752429
                7d40aa29-041e-4383-9bd8-55a8811d11fe
                © 2019 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 21 October 2019
                : 15 November 2019
                Categories
                Article

                Molecular biology
                ageing,autophagy,cell adhesion,cell cycle,circadian rhythm,chromatin remodeling,heat shock factor 1,heat shock proteins,heat shock response,ribosome biogenesis

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