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

Authors
  • Carra, Serena1
  • Alberti, Simon2, 3
  • Benesch, Justin L. P.4
  • Boelens, Wilbert5
  • Buchner, Johannes6
  • Carver, John A.7
  • Cecconi, Ciro8, 9
  • Ecroyd, Heath10, 11
  • Gusev, Nikolai12
  • Hightower, Lawrence E.13
  • Klevit, Rachel E.14
  • Lee, Hyun O.15
  • Liberek, Krzysztof16
  • Lockwood, Brent17
  • Poletti, Angelo18
  • Timmerman, Vincent19
  • Toth, Melinda E.20
  • Vierling, Elizabeth21
  • Wu, Tangchun22
  • Tanguay, Robert M.23
  • 1 University of Modena and Reggio Emilia, Department of Biomedical, Metabolic and Neural Sciences, and Centre for Neuroscience and Nanotechnology, via G. Campi 287, Modena, 41125, Italy , Modena (Italy)
  • 2 Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, 01307, Germany , Dresden (Germany)
  • 3 Technische Universität Dresden, Center for Molecular and Cellular Bioengineering (CMCB), Biotechnology Center (BIOTEC), Tatzberg 47/49, Dresden, 01307, Germany , Dresden (Germany)
  • 4 University of Oxford, Department of Chemistry, Physical and Theoretical Chemistry, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK , Oxford (United Kingdom)
  • 5 Radboud University, Department of Biomolecular Chemistry, Institute of Molecules and Materials, Nijmegen, NL-6500, The Netherlands , Nijmegen (Netherlands)
  • 6 Technische Universität München, Center for Integrated Protein Science Munich (CIPSM) and Department Chemie, Garching, D-85748, Germany , Garching (Germany)
  • 7 The Australian National University, Research School of Chemistry, Acton, ACT, 2601, Australia , Acton (Australia)
  • 8 University of Modena and Reggio Emilia, Department of Physics, Informatics and Mathematics, Modena, 41125, Italy , Modena (Italy)
  • 9 CNR Institute Nanoscience, Center S3, Via Campi 213/A, Modena, 41125, Italy , Modena (Italy)
  • 10 University of Wollongong, School of Chemistry and Molecular Bioscience, Wollongong, NSW, Australia , Wollongong (Australia)
  • 11 Illawarra Health and Medical Research Institute, Wollongong, NSW, Australia , Wollongong (Australia)
  • 12 Moscow State University, Department of Biochemistry, School of Biology, Moscow, 117234, Russian Federation , Moscow (Russia)
  • 13 University of Connecticut, Department of Molecular and Cell Biology, 91 North Eagleville Road, Storrs, CT, 06269-3125, USA , Storrs (United States)
  • 14 University of Washington, Department of Biochemistry, Seattle, WA, USA , Seattle (United States)
  • 15 University of Toronto, Department of Biochemistry, Faculty of Medicine, Toronto, ON, Canada , Toronto (Canada)
  • 16 University of Gdansk, Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology UG-MUG, Abrahama 58, Gdansk, 80-307, Poland , Gdansk (Poland)
  • 17 University of Vermont, Department of Biology, Burlington, VT, 05405, USA , Burlington (United States)
  • 18 Univrsità degli Studi di Milano, Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Centro di Eccellenza sulle Malattie Neurodegenerative, Milan, Italy , Milan (Italy)
  • 19 University of Antwerp, Peripheral Neuropathy Research Group, Department of Biomedical Sciences, Antwerp, 2610, Belgium , Antwerp (Belgium)
  • 20 Biological Research Center, Hungarian Academy of Sciences, Institute of Biochemistry, Szeged, Hungary , Szeged (Hungary)
  • 21 University of Massachusetts Amherst, Department of Biochemistry and Molecular Biology, Amherst, MA, 01003, USA , Amherst (United States)
  • 22 Huazhong University of Science and Technology, MOE Key Lab of Environment and Health, Tongji School of Public Health, 13 Hangkong Rd, Wuhan, Hubei, 430030, China , Wuhan (China)
  • 23 Université Laval, Laboratory of Cell and Developmental Genetics, IBIS, and Department of Molecular Biology, Medical Biochemistry and Pathology, Medical School, QC, Québec, G1V 0A6, Canada , QC (Canada)
Type
Published Article
Journal
Cell Stress and Chaperones
Publisher
Springer Netherlands
Publication Date
Feb 13, 2019
Volume
24
Issue
2
Pages
295–308
Identifiers
DOI: 10.1007/s12192-019-00979-z
Source
Springer Nature
Keywords
License
Yellow

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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