Regulation of the mammalian heat shock factor 1

Sharadha Dayalan Naidu, Albena T. Dinkova-Kostova (Lead / Corresponding author)

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    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 program 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.
    Original languageEnglish
    Pages (from-to)1606-1627
    Number of pages22
    JournalFEBS Journal
    Volume284
    Issue number11
    Early online date4 Jan 2017
    DOIs
    Publication statusPublished - Jun 2017

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    Keywords

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

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