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

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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1007/s12192-019-00979-z

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Oxford college:
University College
Role:
Author


Publisher:
Springer
Journal:
Cell Stress and Chaperones More from this journal
Volume:
24
Issue:
2
Pages:
295-308
Publication date:
2019-02-13
Acceptance date:
2019-02-01
DOI:
EISSN:
1466-1268
ISSN:
1355-8145
Pmid:
30758704


Language:
English
Keywords:
Pubs id:
pubs:975201
UUID:
uuid:6da921eb-e908-4489-8b90-363f1de4c28f
Local pid:
pubs:975201
Source identifiers:
975201
Deposit date:
2019-04-22

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