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The growing world of small heat shock proteins: from structure to functions
- Source :
- Carra, S, Alberti, S, Arrigo, P A, Benesch, J L, Benjamin, I J, Boelens, W, Bartelt-Kirbach, B, Brundel, B J J M, Buchner, J, Bukau, B, Carver, J A, Ecroyd, H, Emanuelsson, C, Finet, S, Golenhofen, N, Goloubinoff, P, Gusev, N, Haslbeck, M, Hightower, L E, Kampinga, H H, Klevit, R E, Liberek, K, Mchaourab, H S, McMenimen, K A, Poletti, A, Quinlan, R, Strelkov, S V, Toth, M E, Vierling, E & Tanguay, R M 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, Cell Stress & Chaperones, 22, 4, pp. 601-611, Cell Stress & Chaperones, 22, 601-611
- Publication Year :
- 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).
- Subjects :
- 0301 basic medicine
Protein aggregates
Heart Diseases
CHAPERONE-LIKE ACTIVITY
Protein Conformation
Cellular differentiation
ALPHA-B-CRYSTALLIN
MYOGENIC DIFFERENTIATION
Protein aggregation
Small heat shock proteins
MIMICKING PHOSPHORYLATION
Biochemistry
03 medical and health sciences
SYNUCLEIN AGGREGATION
Protein Aggregates
Protein structure
DESMIN-RELATED MYOPATHY
Hsp27
Muscular Diseases
Animals
Humans
Small Heat Shock Proteins
Protein Interaction Maps
N-TERMINAL DOMAIN
030102 biochemistry & molecular biology
biology
MOTOR NEUROPATHY
Bio-Molecular Chemistry
Neurodegenerative Diseases
IN-VITRO
Cell Biology
Cell cycle
QUATERNARY ORGANIZATION
Hsp70
Cell biology
Heat-Shock Proteins, Small
030104 developmental biology
Protein conformation
Proteome
biology.protein
Neurological diseases
Protein homeostasis
Function (biology)
Subjects
Details
- Language :
- English
- ISSN :
- 13558145
- Database :
- OpenAIRE
- Journal :
- Carra, S, Alberti, S, Arrigo, P A, Benesch, J L, Benjamin, I J, Boelens, W, Bartelt-Kirbach, B, Brundel, B J J M, Buchner, J, Bukau, B, Carver, J A, Ecroyd, H, Emanuelsson, C, Finet, S, Golenhofen, N, Goloubinoff, P, Gusev, N, Haslbeck, M, Hightower, L E, Kampinga, H H, Klevit, R E, Liberek, K, Mchaourab, H S, McMenimen, K A, Poletti, A, Quinlan, R, Strelkov, S V, Toth, M E, Vierling, E & Tanguay, R M 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, Cell Stress & Chaperones, 22, 4, pp. 601-611, Cell Stress & Chaperones, 22, 601-611
- Accession number :
- edsair.doi.dedup.....c103c1ab0de249cb107b6fcfe3b29a36