title: Small heat-shock proteins: important players in regulating cellular proteostasis.
abstract: 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.
authors.affiliation: Graduate School of Medicine, University of Wollongong, Northfields Avenue, Wollongong, NSW, 2522, Australia. treweek@uow.edu.au.|Illawarra Health and Medical Research Institute, Northfields Avenue, Wollongong, NSW, 2522, Australia. treweek@uow.edu.au.
authors.forename: Teresa M
authors.initials: TM
authors.lastname: Treweek
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
authors.forename: Sarah
authors.initials: S
authors.lastname: Meehan
authors.affiliation: Illawarra Health and Medical Research Institute, Northfields Avenue, Wollongong, NSW, 2522, Australia. heathe@uow.edu.au.|School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW, 2522, Australia. heathe@uow.edu.au.
authors.forename: Heath
authors.initials: H
authors.lastname: Ecroyd
authors.affiliation: Research School of Chemistry, The Australian National University, Acton, ACT, 2601, Australia. john.carver@anu.edu.au.
authors.forename: John A
authors.initials: JA
authors.lastname: Carver
mesh_terms: D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D006706:Homeostasis / Q000235:genetics / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000235:genetics / Q000502:physiology*; D009103:Multiple Sclerosis / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D058105:Polymerization; D066263:Protein Aggregation, Pathological / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000235:genetics / Q000502:physiology*; D038201:alpha-Crystallins / Q000378:metabolism
chemical_list: D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D038201:alpha-Crystallins