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FEBS J. 2017 Jun;284(11):1606-1627. doi: 10.1111/febs.13999. Epub 2017 Feb 1.

Regulation of the mammalian heat shock factor 1.

Author information

1
Division of Cancer Research, School of Medicine, Jacqui Wood Cancer Centre, University of Dundee, UK.
2
Department of Pharmacology and Molecular Sciences, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Abstract

Living organisms are endowed with the capability to tackle various forms of cellular stress due to the presence of molecular chaperone machinery complexes that are ubiquitous throughout the cell. During conditions of proteotoxic stress, the transcription factor heat shock factor 1 (HSF1) mediates the elevation of heat shock proteins, which are crucial components of the chaperone complex machinery and function to ameliorate protein misfolding and aggregation and restore protein homeostasis. In addition, HSF1 orchestrates a versatile transcriptional programme that includes genes involved in repair and clearance of damaged macromolecules and maintenance of cell structure and metabolism, and provides protection against a broad range of cellular stress mediators, beyond heat shock. Here, we discuss the structure and function of the mammalian HSF1 and its regulation by post-translational modifications (phosphorylation, sumoylation and acetylation), proteasomal degradation, and small-molecule activators and inhibitors.

KEYWORDS:

HSF1 activator; HSF1 inhibitor; cytoprotection; hormesis; phytochemical; sulfhydryl reactivity

PMID:
28052564
DOI:
10.1111/febs.13999
[Indexed for MEDLINE]
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