期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 75, 期 16, 页码 2897-2916出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-018-2836-6
关键词
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
资金
- OTKA (Hungarian Scientific Research Fund) [NK78012, K115378]
- MED-inPROT Protein Science Research Synergy Program (Hungarian Academy of Sciences
- HAS)
- VEKOP [VEKOP-2.3.2-16-2017-00014]
- MTA-ELTE Genetics Research Group [01062]
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.
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