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 & 10 others 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

Research output: Contribution to journalReview articleAcademicpeer-review

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).

Original languageEnglish
Pages (from-to)601-611
Number of pages11
JournalCell Stress and Chaperones
Volume22
Issue number4
DOIs
Publication statusPublished - 1 Jul 2017

Cite this

Carra, S., Alberti, S., Arrigo, P. A., Benesch, J. L., Benjamin, I. J., Boelens, W., ... Tanguay, R. M. (2017). The growing world of small heat shock proteins: from structure to functions. Cell Stress and Chaperones, 22(4), 601-611. https://doi.org/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.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. / The growing world of small heat shock proteins : from structure to functions. In: Cell Stress and Chaperones. 2017 ; Vol. 22, No. 4. pp. 601-611.
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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).",
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Carra, S, Alberti, S, Arrigo, PA, Benesch, JL, Benjamin, IJ, Boelens, W, Bartelt-Kirbach, B, Brundel, BJJM, Buchner, J, Bukau, B, Carver, JA, Ecroyd, H, Emanuelsson, C, Finet, S, Golenhofen, N, Goloubinoff, P, Gusev, N, Haslbeck, M, Hightower, LE, Kampinga, HH, Klevit, RE, Liberek, K, Mchaourab, HS, McMenimen, KA, Poletti, A, Quinlan, R, Strelkov, SV, Toth, ME, Vierling, E & Tanguay, RM 2017, 'The growing world of small heat shock proteins: from structure to functions' Cell Stress and Chaperones, vol. 22, no. 4, pp. 601-611. https://doi.org/10.1007/s12192-017-0787-8

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 and Chaperones, Vol. 22, No. 4, 01.07.2017, p. 601-611.

Research output: Contribution to journalReview articleAcademicpeer-review

TY - JOUR

T1 - The growing world of small heat shock proteins

T2 - from structure to functions

AU - Carra, Serena

AU - Alberti, Simon

AU - Arrigo, Patrick A.

AU - Benesch, Justin L.

AU - Benjamin, Ivor J.

AU - Boelens, Wilbert

AU - Bartelt-Kirbach, Britta

AU - Brundel, Bianca J.J.M.

AU - Buchner, Johannes

AU - Bukau, Bernd

AU - Carver, John A.

AU - Ecroyd, Heath

AU - Emanuelsson, Cecilia

AU - Finet, Stephanie

AU - Golenhofen, Nikola

AU - Goloubinoff, Pierre

AU - Gusev, Nikolai

AU - Haslbeck, Martin

AU - Hightower, Lawrence E.

AU - Kampinga, Harm H.

AU - Klevit, Rachel E.

AU - Liberek, Krzysztof

AU - Mchaourab, Hassane S.

AU - McMenimen, Kathryn A.

AU - Poletti, Angelo

AU - Quinlan, Roy

AU - Strelkov, Sergei V.

AU - Toth, Melinda E.

AU - Vierling, Elizabeth

AU - Tanguay, Robert M.

PY - 2017/7/1

Y1 - 2017/7/1

N2 - 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).

AB - 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).

KW - Hsp27

KW - Neurological diseases

KW - Protein aggregates

KW - Protein conformation

KW - Protein homeostasis

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Carra S, Alberti S, Arrigo PA, Benesch JL, Benjamin IJ, Boelens W et al. The growing world of small heat shock proteins: from structure to functions. Cell Stress and Chaperones. 2017 Jul 1;22(4):601-611. https://doi.org/10.1007/s12192-017-0787-8