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Cell Stress Chaperones. 2019 Mar;24(2):295-308. doi: 10.1007/s12192-019-00979-z. Epub 2019 Feb 13.

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

Author information

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@unimore.it.
2
Max Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.
3
Center for Molecular and Cellular Bioengineering (CMCB), Biotechnology Center (BIOTEC), Technische Universität Dresden, Tatzberg 47/49, 01307, Dresden, Germany.
4
Department of Chemistry, Physical and Theoretical Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK.
5
Department of Biomolecular Chemistry, Institute of Molecules and Materials, Radboud University, NL-6500, Nijmegen, The Netherlands.
6
Center for Integrated Protein Science Munich (CIPSM) and Department Chemie, Technische Universität München, D-85748, Garching, Germany.
7
Research School of Chemistry, The Australian National University, Acton, ACT, 2601, Australia.
8
Department of Physics, Informatics and Mathematics, University of Modena and Reggio Emilia, 41125, Modena, Italy.
9
Center S3, CNR Institute Nanoscience, Via Campi 213/A, 41125, Modena, Italy.
10
School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, NSW, Australia.
11
Illawarra Health and Medical Research Institute, Wollongong, NSW, Australia.
12
Department of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation, 117234.
13
Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT, 06269-3125, USA.
14
Department of Biochemistry, University of Washington, Seattle, WA, USA.
15
Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, ON, Canada.
16
Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology UG-MUG, University of Gdansk, Abrahama 58, 80-307, Gdansk, Poland.
17
Department of Biology, University of Vermont, Burlington, VT, 05405, USA.
18
Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Centro di Eccellenza sulle Malattie Neurodegenerative, Univrsità degli Studi di Milano, Milan, Italy.
19
Peripheral Neuropathy Research Group, Department of Biomedical Sciences, University of Antwerp, 2610, Antwerp, Belgium.
20
Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
21
Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
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.
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.tanguay@fmed.ulaval.ca.

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.

KEYWORDS:

Human diseases; Plant biology; Protein quality control; Small heat shock proteins

PMID:
30758704
PMCID:
PMC6439001
[Available on 2019-09-01]
DOI:
10.1007/s12192-019-00979-z

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