Small heat-shock proteins: Important players in regulating cellular proteostasis

Teresa M. Treweek*, Sarah Meehan, Heath Ecroyd, John A. Carver

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    166 Citations (Scopus)


    Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease.

    Original languageEnglish
    Pages (from-to)429-451
    Number of pages23
    JournalCellular and Molecular Life Sciences
    Issue number3
    Publication statusPublished - Feb 2015


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