Roles of heat shock factor 1 beyond the heat shock response

János Barna, P. Csermely, T. Vellai

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Various stress factors leading to protein damage induce the activation of an evolutionarily conserved cell protective mechanism, the heat shock response (HSR), to maintain protein homeostasis in virtually all eukaryotic cells. Heat shock factor 1 (HSF1) plays a central role in the HSR. HSF1 was initially known as a transcription factor that upregulates genes encoding heat shock proteins (HSPs), also called molecular chaperones, which assist in refolding or degrading injured intracellular proteins. However, recent accumulating evidence indicates multiple additional functions for HSF1 beyond the activation of HSPs. Here, we present a nearly comprehensive list of non-HSP-related target genes of HSF1 identified so far. Through controlling these targets, HSF1 acts in diverse stress-induced cellular processes and molecular mechanisms, including the endoplasmic reticulum unfolded protein response and ubiquitin–proteasome system, multidrug resistance, autophagy, apoptosis, immune response, cell growth arrest, differentiation underlying developmental diapause, chromatin remodelling, cancer development, and ageing. Hence, HSF1 emerges as a major orchestrator of cellular stress response pathways.

Original languageEnglish
Pages (from-to)1-20
Number of pages20
JournalCellular and Molecular Life Sciences
DOIs
Publication statusAccepted/In press - May 17 2018

Fingerprint

Heat-Shock Response
Shock
Hot Temperature
Heat-Shock Proteins
Proteins
Unfolded Protein Response
Molecular Chaperones
Chromatin Assembly and Disassembly
Autophagy
Multiple Drug Resistance
Eukaryotic Cells
Endoplasmic Reticulum
Genes
Homeostasis
Transcription Factors
Up-Regulation
Apoptosis
Growth

Keywords

  • Ageing
  • Apoptosis
  • Autophagy
  • Cancer
  • Cell cycle
  • Circadian rhythm
  • Development
  • Differentiation
  • Heat shock factor 1
  • Heat shock proteins
  • Heat shock response
  • Immune response
  • Multidrug resistance
  • Oxidative stress
  • Proteasome
  • Unfolded protein response

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

Roles of heat shock factor 1 beyond the heat shock response. / Barna, János; Csermely, P.; Vellai, T.

In: Cellular and Molecular Life Sciences, 17.05.2018, p. 1-20.

Research output: Contribution to journalArticle

@article{3a27abd9282e4c548c792d9d909f6af5,
title = "Roles of heat shock factor 1 beyond the heat shock response",
abstract = "Various stress factors leading to protein damage induce the activation of an evolutionarily conserved cell protective mechanism, the heat shock response (HSR), to maintain protein homeostasis in virtually all eukaryotic cells. Heat shock factor 1 (HSF1) plays a central role in the HSR. HSF1 was initially known as a transcription factor that upregulates genes encoding heat shock proteins (HSPs), also called molecular chaperones, which assist in refolding or degrading injured intracellular proteins. However, recent accumulating evidence indicates multiple additional functions for HSF1 beyond the activation of HSPs. Here, we present a nearly comprehensive list of non-HSP-related target genes of HSF1 identified so far. Through controlling these targets, HSF1 acts in diverse stress-induced cellular processes and molecular mechanisms, including the endoplasmic reticulum unfolded protein response and ubiquitin–proteasome system, multidrug resistance, autophagy, apoptosis, immune response, cell growth arrest, differentiation underlying developmental diapause, chromatin remodelling, cancer development, and ageing. Hence, HSF1 emerges as a major orchestrator of cellular stress response pathways.",
keywords = "Ageing, Apoptosis, Autophagy, Cancer, Cell cycle, Circadian rhythm, Development, Differentiation, Heat shock factor 1, Heat shock proteins, Heat shock response, Immune response, Multidrug resistance, Oxidative stress, Proteasome, Unfolded protein response",
author = "J{\'a}nos Barna and P. Csermely and T. Vellai",
year = "2018",
month = "5",
day = "17",
doi = "10.1007/s00018-018-2836-6",
language = "English",
pages = "1--20",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-682X",
publisher = "Birkhauser Verlag Basel",

}

TY - JOUR

T1 - Roles of heat shock factor 1 beyond the heat shock response

AU - Barna, János

AU - Csermely, P.

AU - Vellai, T.

PY - 2018/5/17

Y1 - 2018/5/17

N2 - Various stress factors leading to protein damage induce the activation of an evolutionarily conserved cell protective mechanism, the heat shock response (HSR), to maintain protein homeostasis in virtually all eukaryotic cells. Heat shock factor 1 (HSF1) plays a central role in the HSR. HSF1 was initially known as a transcription factor that upregulates genes encoding heat shock proteins (HSPs), also called molecular chaperones, which assist in refolding or degrading injured intracellular proteins. However, recent accumulating evidence indicates multiple additional functions for HSF1 beyond the activation of HSPs. Here, we present a nearly comprehensive list of non-HSP-related target genes of HSF1 identified so far. Through controlling these targets, HSF1 acts in diverse stress-induced cellular processes and molecular mechanisms, including the endoplasmic reticulum unfolded protein response and ubiquitin–proteasome system, multidrug resistance, autophagy, apoptosis, immune response, cell growth arrest, differentiation underlying developmental diapause, chromatin remodelling, cancer development, and ageing. Hence, HSF1 emerges as a major orchestrator of cellular stress response pathways.

AB - Various stress factors leading to protein damage induce the activation of an evolutionarily conserved cell protective mechanism, the heat shock response (HSR), to maintain protein homeostasis in virtually all eukaryotic cells. Heat shock factor 1 (HSF1) plays a central role in the HSR. HSF1 was initially known as a transcription factor that upregulates genes encoding heat shock proteins (HSPs), also called molecular chaperones, which assist in refolding or degrading injured intracellular proteins. However, recent accumulating evidence indicates multiple additional functions for HSF1 beyond the activation of HSPs. Here, we present a nearly comprehensive list of non-HSP-related target genes of HSF1 identified so far. Through controlling these targets, HSF1 acts in diverse stress-induced cellular processes and molecular mechanisms, including the endoplasmic reticulum unfolded protein response and ubiquitin–proteasome system, multidrug resistance, autophagy, apoptosis, immune response, cell growth arrest, differentiation underlying developmental diapause, chromatin remodelling, cancer development, and ageing. Hence, HSF1 emerges as a major orchestrator of cellular stress response pathways.

KW - Ageing

KW - Apoptosis

KW - Autophagy

KW - Cancer

KW - Cell cycle

KW - Circadian rhythm

KW - Development

KW - Differentiation

KW - Heat shock factor 1

KW - Heat shock proteins

KW - Heat shock response

KW - Immune response

KW - Multidrug resistance

KW - Oxidative stress

KW - Proteasome

KW - Unfolded protein response

UR - http://www.scopus.com/inward/record.url?scp=85047147425&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85047147425&partnerID=8YFLogxK

U2 - 10.1007/s00018-018-2836-6

DO - 10.1007/s00018-018-2836-6

M3 - Article

C2 - 29774376

AN - SCOPUS:85047147425

SP - 1

EP - 20

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

ER -