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).

The growing world of small heat shock proteins: from structure to functions / Carra, Serena; Alberti, Simon; Arrigo, Patrick A.; Benesch, Justin L.; Benjamin, Ivor J.; Boelens, Wilbert; Bartelt-Kirbach, Britta; Brundel, Bianca J. J. M.; Buchner, Johannes; Bukau, Bernd; Carver, John A.; Ecroyd, Heath; Emanuelsson, Cecilia; Finet, Stephanie; Golenhofen, Nikola; Goloubinoff, Pierre; Gusev, Nikolai; Haslbeck, Martin; Hightower, Lawrence E.; Kampinga, Harm H.; Klevit, Rachel E.; Liberek, Krzysztof; Mchaourab, Hassane S.; Mcmenimen, Kathryn A.; Poletti, Angelo; Quinlan, Roy; Strelkov, Sergei V.; Toth, Melinda E.; Vierling, Elizabeth; Tanguay, Robert M.. - In: CELL STRESS & CHAPERONES. - ISSN 1355-8145. - 22:4(2017), pp. 601-611. [10.1007/s12192-017-0787-8]

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

Carra, Serena
Writing – Original Draft Preparation
;
2017

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).
2017
31-mar-2017
22
4
601
611
The growing world of small heat shock proteins: from structure to functions / Carra, Serena; Alberti, Simon; Arrigo, Patrick A.; Benesch, Justin L.; Benjamin, Ivor J.; Boelens, Wilbert; Bartelt-Kirbach, Britta; Brundel, Bianca J. J. M.; Buchner, Johannes; Bukau, Bernd; Carver, John A.; Ecroyd, Heath; Emanuelsson, Cecilia; Finet, Stephanie; Golenhofen, Nikola; Goloubinoff, Pierre; Gusev, Nikolai; Haslbeck, Martin; Hightower, Lawrence E.; Kampinga, Harm H.; Klevit, Rachel E.; Liberek, Krzysztof; Mchaourab, Hassane S.; Mcmenimen, Kathryn A.; Poletti, Angelo; Quinlan, Roy; Strelkov, Sergei V.; Toth, Melinda E.; Vierling, Elizabeth; Tanguay, Robert M.. - In: CELL STRESS & CHAPERONES. - ISSN 1355-8145. - 22:4(2017), pp. 601-611. [10.1007/s12192-017-0787-8]
Carra, Serena; Alberti, Simon; Arrigo, Patrick A.; Benesch, Justin L.; Benjamin, Ivor J.; Boelens, Wilbert; Bartelt-Kirbach, Britta; Brundel, Bianca J...espandi
File in questo prodotto:
File Dimensione Formato  
Carra et al 2017.pdf

Accesso riservato

Tipologia: Versione pubblicata dall'editore
Dimensione 400.71 kB
Formato Adobe PDF
400.71 kB Adobe PDF   Visualizza/Apri   Richiedi una copia
Pubblicazioni consigliate

Licenza Creative Commons
I metadati presenti in IRIS UNIMORE sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono rilasciati con licenza Attribuzione 4.0 Internazionale (CC BY 4.0), salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/1152766
Citazioni
  • ???jsp.display-item.citation.pmc??? 78
  • Scopus 127
  • ???jsp.display-item.citation.isi??? 128
social impact