title: Polyglutamine aggregation in Huntington and related diseases.
abstract: Polyglutamine (polyQ)-expansions in different proteins cause nine neurodegenerative diseases. While polyQ aggregation is a key pathological hallmark of these diseases, how aggregation relates to pathogenesis remains contentious. In this chapter, we review what is known about the aggregation process and how cells respond and interact with the polyQ-expanded proteins. We cover detailed biophysical and structural studies to uncover the intrinsic features of polyQ aggregates and concomitant effects in the cellular environment. We also examine the functional consequences ofpolyQ aggregation and how cells may attempt to intervene and guide the aggregation process.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Victoria, Australia.
authors.forename: Saskia
authors.initials: S
authors.lastname: Polling
authors.forename: Andrew F
authors.initials: AF
authors.lastname: Hill
authors.forename: Danny M
authors.initials: DM
authors.lastname: Hatters
mesh_terms: D060833:Cellular Microenvironment; D006801:Humans; D006816:Huntington Disease / Q000235:genetics / Q000378:metabolism* / Q000503:physiopathology; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D057165:Proteostasis Deficiencies / Q000235:genetics / Q000378:metabolism* / Q000503:physiopathology
chemical_list: D010455:Peptides; C097188:polyglutamine