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Small heat shock proteins: multifaceted proteins with important implications for life

  • Meeting Review
  • Published:
Cell Stress and Chaperones Aims and scope

Abstract

Small Heat Shock Proteins (sHSPs) evolved early in the history of life; they are present in archaea, bacteria, and eukaryota. sHSPs belong to the superfamily of molecular chaperones: they are components of the cellular protein quality control machinery and are thought to act as the first line of defense against conditions that endanger the cellular proteome. In plants, sHSPs protect cells against abiotic stresses, providing innovative targets for sustainable agricultural production. In humans, sHSPs (also known as HSPBs) are associated with the development of several neurological diseases. Thus, manipulation of sHSP expression may represent an attractive therapeutic strategy for disease treatment. Experimental evidence demonstrates that enhancing the chaperone function of sHSPs protects against age-related protein conformation diseases, which are characterized by protein aggregation. Moreover, sHSPs can promote longevity and healthy aging in vivo. In addition, sHSPs have been implicated in the prognosis of several types of cancer. Here, sHSP upregulation, by enhancing cellular health, could promote cancer development; on the other hand, their downregulation, by sensitizing cells to external stressors and chemotherapeutics, may have beneficial outcomes. The complexity and diversity of sHSP function and properties and the need to identify their specific clients, as well as their implication in human disease, have been discussed by many of the world’s experts in the sHSP field during a dedicated workshop in Québec City, Canada, on 26–29 August 2018.

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Acknowledgements

We are grateful to the Cell Stress Society International (CSSI) for its financial support of the workshop. We thank the Fund for Scientific Research in Flanders-Belgium (FWO) for supporting the attendance at the workshop of PhD students, Elias Adriaenssens and Leen Vendredy.

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Authors and Affiliations

  1. Department of Biomedical, Metabolic and Neural Sciences, and Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, via G. Campi 287, 41125, Modena, Italy

    Serena Carra

  2. Max Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany

    Simon Alberti

  3. Center for Molecular and Cellular Bioengineering (CMCB), Biotechnology Center (BIOTEC), Technische Universität Dresden, Tatzberg 47/49, 01307, Dresden, Germany

    Simon Alberti

  4. Department of Chemistry, Physical and Theoretical Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK

    Justin L. P. Benesch

  5. Department of Biomolecular Chemistry, Institute of Molecules and Materials, Radboud University, NL-6500, Nijmegen, The Netherlands

    Wilbert Boelens

  6. Center for Integrated Protein Science Munich (CIPSM) and Department Chemie, Technische Universität München, D-85748, Garching, Germany

    Johannes Buchner

  7. Research School of Chemistry, The Australian National University, Acton, ACT, 2601, Australia

    John A. Carver

  8. Department of Physics, Informatics and Mathematics, University of Modena and Reggio Emilia, 41125, Modena, Italy

    Ciro Cecconi

  9. Center S3, CNR Institute Nanoscience, Via Campi 213/A, 41125, Modena, Italy

    Ciro Cecconi

  10. School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW, Australia

    Heath Ecroyd

  11. Illawarra Health and Medical Research Institute, Wollongong, NSW, Australia

    Heath Ecroyd

  12. Department of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation, 117234

    Nikolai Gusev

  13. Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT, 06269-3125, USA

    Lawrence E. Hightower

  14. Department of Biochemistry, University of Washington, Seattle, WA, USA

    Rachel E. Klevit

  15. Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, ON, Canada

    Hyun O. Lee

  16. Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology UG-MUG, University of Gdansk, Abrahama 58, 80-307, Gdansk, Poland

    Krzysztof Liberek

  17. Department of Biology, University of Vermont, Burlington, VT, 05405, USA

    Brent Lockwood

  18. Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Centro di Eccellenza sulle Malattie Neurodegenerative, Univrsità degli Studi di Milano, Milan, Italy

    Angelo Poletti

  19. Peripheral Neuropathy Research Group, Department of Biomedical Sciences, University of Antwerp, 2610, Antwerp, Belgium

    Vincent Timmerman

  20. Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary

    Melinda E. Toth

  21. Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA, 01003, USA

    Elizabeth Vierling

  22. MOE Key Lab of Environment and Health, Tongji School of Public Health, Huazhong University of Science and Technology, 13 Hangkong Rd, Wuhan, 430030, Hubei, China

    Tangchun Wu

  23. Laboratory of Cell and Developmental Genetics, IBIS, and Department of Molecular Biology, Medical Biochemistry and Pathology, Medical School, Université Laval, QC, Québec, G1V 0A6, Canada

    Robert M. Tanguay

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  1. Serena Carra
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Correspondence to Serena Carra or Robert M. Tanguay.

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Carra, S., Alberti, S., Benesch, J.L.P. et al. Small heat shock proteins: multifaceted proteins with important implications for life. Cell Stress and Chaperones 24, 295–308 (2019). https://doi.org/10.1007/s12192-019-00979-z

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