title: Assays to monitor aggrephagy.
abstract: The presence of ubiquitinated protein inclusions is a hallmark of most adult onset neurodegenerative disorders. Results from several neurodegenerative model systems indicate that elimination of the disease-associated inclusions can lead to symptomatic reversal, and a better understanding of the mechanisms involved in accumulation and turnover of aggregation-prone proteins is therefore important. Autophagy has been found to contribute to protein aggregate clearance, and the term aggrephagy is used to describe the selective degradation of aggregation-prone proteins by autophagy. Here, we provide an overview of different disease-related model systems and assays that can be used to distinguish non-aggregated from aggregation-prone proteins, and how these assays can be used to determine turnover of protein aggregates by autophagy.
authors.affiliation: Institute of Basic Medical Sciences, University of Oslo, Norway.
authors.forename: Alf Håkon
authors.initials: AH
authors.lastname: Lystad
authors.affiliation: Institute of Basic Medical Sciences, University of Oslo, Norway. Electronic address: anne.simonsen@medisin.uio.no.
authors.forename: Anne
authors.initials: A
authors.lastname: Simonsen
mesh_terms: D001343:Autophagy / Q000235:genetics*; D001681:Biological Assay / Q000379:methods*; D006801:Humans; D009410:Nerve Degeneration / Q000235:genetics* / Q000473:pathology; D019636:Neurodegenerative Diseases / Q000235:genetics* / Q000473:pathology; D066263:Protein Aggregation, Pathological / Q000235:genetics; D054875:Ubiquitination / Q000235:genetics
keywords: Aggrephagy; Autophagy; Neurodegeneration; PolyQ; UPS; p62