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

被引：0
作者：
Serena Carra
Simon Alberti
Justin L. P. Benesch
Wilbert Boelens
Johannes Buchner
John A. Carver
Ciro Cecconi
Heath Ecroyd
Nikolai Gusev
Lawrence E. Hightower
Rachel E. Klevit
Hyun O. Lee
Krzysztof Liberek
Brent Lockwood
Angelo Poletti
Vincent Timmerman
Melinda E. Toth
Elizabeth Vierling
Tangchun Wu
Robert M. Tanguay
机构：
[1] University of Modena and Reggio Emilia,Department of Biomedical, Metabolic and Neural Sciences, and Centre for Neuroscience and Nanotechnology
[2] Max Planck Institute of Molecular Cell Biology and Genetics,Center for Molecular and Cellular Bioengineering (CMCB), Biotechnology Center (BIOTEC)
[3] Technische Universität Dresden,Department of Chemistry, Physical and Theoretical Chemistry, Chemistry Research Laboratory
[4] University of Oxford,Department of Biomolecular Chemistry, Institute of Molecules and Materials
[5] Radboud University,Center for Integrated Protein Science Munich (CIPSM) and Department Chemie
[6] Technische Universität München,Research School of Chemistry
[7] The Australian National University,Department of Physics, Informatics and Mathematics
[8] University of Modena and Reggio Emilia,Center S3
[9] CNR Institute Nanoscience,School of Chemistry and Molecular Bioscience
[10] University of Wollongong,Department of Biochemistry, School of Biology
[11] Illawarra Health and Medical Research Institute,Department of Molecular and Cell Biology
[12] Moscow State University,Department of Biochemistry
[13] University of Connecticut,Department of Biochemistry, Faculty of Medicine
[14] University of Washington,Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology UG
[15] University of Toronto,MUG
[16] University of Gdansk,Department of Biology
[17] University of Vermont,Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Centro di Eccellenza sulle Malattie Neurodegenerative
[18] Univrsità degli Studi di Milano,Peripheral Neuropathy Research Group, Department of Biomedical Sciences
[19] University of Antwerp,Institute of Biochemistry
[20] Biological Research Center,Department of Biochemistry and Molecular Biology
[21] Hungarian Academy of Sciences,MOE Key Lab of Environment and Health, Tongji School of Public Health
[22] University of Massachusetts Amherst,Laboratory of Cell and Developmental Genetics, IBIS, and Department of Molecular Biology, Medical Biochemistry and Pathology, Medical School
[23] Huazhong University of Science and Technology,undefined
[24] Université Laval,undefined
来源：
Cell Stress and Chaperones | 2019年 / 24卷
关键词：
Small heat shock proteins; Protein quality control; Human diseases; Plant biology;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
引用
收藏
页码：295 / 308
页数：13
相关论文
共 895 条
[1]  
Adhikari AS(2004)Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for alphaB-crystallin and Hsp25 Exp Cell Res 299 393-403
[2]  
Sridhar Rao K(2011)Physical exercise as a preventive or disease-modifying treatment of dementia and brain aging Mayo Clin Proc 86 876-884
[3]  
Rangaraj N(2017)Phase separation in biology Curr Biol 27 R1097-R1102
[4]  
Parnaik VK(2017)Granulostasis: protein quality control of RNP granules Front Mol Neurosci 10 84-28680
[5]  
Mohan Rao C(2004)Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure J Biol Chem 279 28675-148
[6]  
Ahlskog JE(2010)Chaperone-assisted selective autophagy is essential for muscle maintenance Curr Biol 20 143-288
[7]  
Geda YE(2000)sHsp as novel regulators of programmed cell death and tumorigenicity Pathologie-biologie 48 280-1255
[8]  
Graff-Radford NR(2002)Expression of the anti-apoptotic protein Hsp27 during both the keratinocyte differentiation and dedifferentiation of HaCat cells: expression linked to changes in intracellular protein organization? Exp Gerontol 37 1247-1163
[9]  
Petersen RC(2012)HspB1 dynamic phospho-oligomeric structure dependent interactome as cancer therapeutic target Curr Mol Med 12 1151-365
[10]  
Alberti S(2014)HspB1, HspB5 and HspB4 in human cancers: potent oncogenic role of some of their client proteins Cancers 6 333-5071
12345678910