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

Serena Carra , Simon Alberti , Patrick A. Arrigo , Justin L. Benesch , Ivor J. Benjamin , Wilbert Boelens , Britta Bartelt-Kirbach , Bianca J. J. M. Brundel , Johannes Buchner , Bernd Bukau , John A. Carver , Heath Ecroyd , Cecilia Emanuelsson , Stephanie Finet , Nikola Golenhofen , Pierre Goloubinoff , Nikolai Gusev , Martin Haslbeck , Lawrence E. Hightower , Harm H. Kampinga , Rachel E. Klevit , Krzysztof Liberek , Hassane S. Mchaourab , Kathryn A. McMenimen , Angelo Poletti , Roy Quinlan , Sergei V. Strelkov , Melinda E. Toth , Elizabeth Vierling , Robert M. Tanguay

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 orga- nized in Italy (Bertinoro, CEUB, October 12–15, 2016).
Author Serena Carra
Serena Carra,,
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, Simon Alberti
Simon Alberti,,
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, Patrick A. Arrigo
Patrick A. Arrigo,,
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, Justin L. Benesch
Justin L. Benesch,,
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, Ivor J. Benjamin
Ivor J. Benjamin,,
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, Wilbert Boelens
Wilbert Boelens,,
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, Britta Bartelt-Kirbach
Britta Bartelt-Kirbach,,
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, Bianca J. J. M. Brundel
Bianca J. J. M. Brundel,,
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, Johannes Buchner
Johannes Buchner,,
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, Bernd Bukau
Bernd Bukau,,
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et al.
Journal seriesCell Stress & Chaperones, ISSN 1355-8145
Issue year2017
Vol22
No4
Pages601-611
Publication size in sheets0.5
Keywords in Englishsmall heat shock proteins, Hsp27, protein conformation, neurological diseases, protein homeostasis, protein aggregates
DOIDOI:10.1007/s12192-017-0787-8
URL https://link.springer.com/content/pdf/10.1007%2Fs12192-017-0787-8.pdf
Languageen angielski
Score (nominal)25
ScoreMinisterial score = 20.0, 26-01-2018, ArticleFromJournal
Ministerial score (2013-2016) = 25.0, 26-01-2018, ArticleFromJournal
Publication indicators WoS Impact Factor: 2016 = 2.411 (2) - 2016=2.571 (5)
Citation count*0
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