The growing world of small heat shock proteins: from structure to functions

Serena Carra, Simon Alberti, Patrick A. Arrigo, Justin L. Benesch, Ivor J. Benjamin, Wilbert Boelens, Britta Bartelt-Kirbach, Bianca J.J.M. Brundel, Johannes Buchner, Bernd Bukau, John A. Carver, Heath Ecroyd, Cecilia Emanuelsson, Stephanie Finet, Nikola Golenhofen, Pierre Goloubinoff, Nikolai Gusev, Martin Haslbeck, Lawrence E. Hightower, Harm H. KampingaRachel E. Klevit, Krzysztof Liberek, Hassane S. Mchaourab, Kathryn A. McMenimen, Angelo Poletti, Roy Quinlan, Sergei V. Strelkov, Melinda E. Toth, Elizabeth Vierling, Robert M. Tanguay*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental roles in cell biology. sHSPs are key components of the cellular protein quality control system, acting as the first line of defense against conditions that affect protein homeostasis and proteome stability, from bacteria to plants to humans. sHSPs have the ability to bind to a large subset of substrates and to maintain them in a state competent for refolding or clearance with the assistance of the HSP70 machinery. sHSPs participate in a number of biological processes, from the cell cycle, to cell differentiation, from adaptation to stressful conditions, to apoptosis, and, even, to the transformation of a cell into a malignant state. As a consequence, sHSP malfunction has been implicated in abnormal placental development and preterm deliveries, in the prognosis of several types of cancer, and in the development of neurological diseases. Moreover, mutations in the genes encoding several mammalian sHSPs result in neurological, muscular, or cardiac age-related diseases in humans. Loss of protein homeostasis due to protein aggregation is typical of many age-related neurodegenerative and neuromuscular diseases. In light of the role of sHSPs in the clearance of un/misfolded aggregation-prone substrates, pharmacological modulation of sHSP expression or function and rescue of defective sHSPs represent possible routes to alleviate or cure protein conformation diseases. Here, we report the latest news and views on sHSPs discussed by many of the world’s experts in the sHSP field during a dedicated workshop organized in Italy (Bertinoro, CEUB, October 12–15, 2016).

Original languageEnglish
Pages (from-to)601-611
Number of pages11
JournalCell Stress and Chaperones
Issue number4
StatePublished - 1 Jul 2017
Externally publishedYes


FundersFunder number
National Institute of General Medical SciencesR15GM120654
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung156948


    • Hsp27
    • Neurological diseases
    • Protein aggregates
    • Protein conformation
    • Protein homeostasis
    • Small heat shock proteins


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