caa a22 4500 606175946 CHVBK 20210128100745.0 cr unu---uuuuu 210128e20150201xx s 000 0 eng 10.1007/s00018-014-1754-5 doi (NATIONALLICENCE)springer-10.1007/s00018-014-1754-5 Small heat-shock proteins: important players in regulating cellular proteostasis [Elektronische Daten] [Teresa Treweek, Sarah Meehan, Heath Ecroyd, John Carver] Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease. Springer Basel, 2014 Small heat-shock protein nationallicence Protein aggregation nationallicence Molecular chaperone nationallicence Proteostasis nationallicence Cataract nationallicence Neurodegenerative disease nationallicence Aβ : Amyloid β nationallicence αAc : αA-crystallin nationallicence αBc : αB-crystallin nationallicence αc : α-Crystallin nationallicence ACD : α-Crystallin domain nationallicence AD : Alzheimer's disease nationallicence ALS : Amylotrophic lateral sclerosis nationallicence α-syn : α-Synuclein nationallicence CJD : Creutzfeldt-Jakob disease nationallicence CMT : Charcot-Marie-Tooth disease nationallicence cryo-EM : Cryo-electron microscopy nationallicence DRM : Desmin-related myopathy nationallicence GAFP : Glial acidic fibrillary protein nationallicence HMN : Hereditary motor neuropathy nationallicence Hsp : Heat-shock protein nationallicence MS : Multiple sclerosis nationallicence PD : Parkinson's disease nationallicence PrPsc : Prion protein nationallicence SANS : Small-angle neutron scattering nationallicence SAXS : Small-angle X-ray scattering nationallicence sHsp : Small heat-shock protein nationallicence TEM : Transmission electron microscopy nationallicence Treweek Teresa Graduate School of Medicine, University of Wollongong, Northfields Avenue, 2522, Wollongong, NSW, Australia aut Meehan Sarah Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut Ecroyd Heath Illawarra Health and Medical Research Institute, Northfields Avenue, 2522, Wollongong, NSW, Australia aut Carver John Research School of Chemistry, The Australian National University, 2601, Acton, ACT, Australia aut Cellular and Molecular Life Sciences Springer Basel 72/3(2015-02-01), 429-451 1420-682X 72:3<429 2015 72 18 https://doi.org/10.1007/s00018-014-1754-5 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-014-1754-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Treweek Teresa Graduate School of Medicine, University of Wollongong, Northfields Avenue, 2522, Wollongong, NSW, Australia aut NATIONALLICENCE 700 1- Meehan Sarah Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW, Cambridge, UK aut NATIONALLICENCE 700 1- Ecroyd Heath Illawarra Health and Medical Research Institute, Northfields Avenue, 2522, Wollongong, NSW, Australia aut NATIONALLICENCE 700 1- Carver John Research School of Chemistry, The Australian National University, 2601, Acton, ACT, Australia aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/3(2015-02-01), 429-451 1420-682X 72:3<429 2015 72 18