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Cell Stress Chaperones. 2017 Jul;22(4):601-611. doi: 10.1007/s12192-017-0787-8. Epub 2017 Mar 31.

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

Author information

1
Department of Biomedical, Metabolic and Neural Sciences, and Centre for Neuroscience and Neurotechnology, University of Modena and Reggio Emilia, via G. Campi 287, 41125, Modena, Italy.
2
Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
3
Université de Lyon, 69622, Lyon, France.
4
CNRS, UMR 5310, INSERM U1217, Institut NeuroMyoGène, Université Lyon 1, 69100, Villeurbanne, France.
5
Department of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.
6
Department of Biochemistry, University of Utah, Salt Lake City, UT, 84112-5650, USA.
7
Biomolecular Chemistry, 284, Radboud University, PO Box 9101, 6500 HB, Nijmegen, The Netherlands.
8
Institute of Anatomy and Cell Biology, University of Ulm, 89081, Ulm, Germany.
9
Department of Clinical Pharmacy and Pharmacology, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.
10
Department of Physiology, Institute for Cardiovascular Research, VU University Medical Center, Amsterdam, The Netherlands.
11
Technische Universitat Munchen, Munich, Germany.
12
Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany.
13
German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120, Heidelberg, Germany.
14
The Research School of Chemistry, The Australian National University, Acton, ACT, 2601, Australia.
15
Illawara Health and Medical Research Institute, School of Biological Sciences, University of Wollongong, Wollongong, NSW, 2522, Australia.
16
Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, 221 00, Lund, Sweden.
17
IMPMC UMR7590, CNRS, UPMC Paris 6, 4 place Jussieu, Paris, France.
18
Department of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.
19
Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119991, Russia.
20
Department of Molecular & Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT, 06269-3125, USA.
21
Department of Cell Biology, University Medical Center Groningen, University of Groningen, 9713 GZ, Groningen, The Netherlands.
22
Department of Biochemistry, University of Washington, Seattle, WA, 98195, USA.
23
Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology, University of Gdańsk and the Medical University of Gdańsk, Gdańsk, Poland.
24
Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, 37232, USA.
25
Departments of Pathology, Biological Chemistry, and Medicinal Chemistry and the Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA.
26
Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Centro di Eccellenza sulle Malattie Neurodegenerative, Università degli Studi di Milano, Milan, Italy.
27
Department of Biosciences and the Biophysical Sciences Institute, University of Durham, Durham, UK.
28
Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Leuven, Belgium.
29
Laboratory of Animal Genetics and Molecular Neurobiology, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary.
30
Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
31
Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, 85721, USA.
32
Laboratory of Cell & Developmental Genetics, IBIS, and Department of Molecular Biology, Medical Biochemistry and Pathology, Medical School, Université Laval, Québec (Qc), G1V 0A6, Canada. Robert.tanguay@fmed.ulaval.ca.

Abstract

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).

KEYWORDS:

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

PMID:
28364346
PMCID:
PMC5465036
DOI:
10.1007/s12192-017-0787-8
[Indexed for MEDLINE]
Free PMC Article

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