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- W157037429 abstract "AbstractProtein aggregation as a result of misfolding is a common theme underlying neurodegenerative diseases. Although a subject of intense research, how misfolded proteins bypass sophisticated protein quality control measures in the cell to be deposited as ubiquitin-enriched inclusion bodies remains poorly understood. Whilst proteasome dysfunction could account for this phenomenon, emerging evidence suggests otherwise. We have previously hypothesized that under conditions of proteolytic stress, the cell may switch to a non-proteolytic form of ubiquitination to help divert misfolded proteins away from an overloaded proteasome. In this way, the cell could preserve its proteasome function over prolonged periods of stress and recover thereafter. Supporting this, we recently found that non-proteolytic lysine (K) 63-linked ubiquitin modification promotes the formation of protein inclusions associated with several major neurodegenerative diseases. Importantly, we further found that K63-linked polyubiquitin selectively facilitates the subsequent clearance of inclusions via autophagy. In this chapter, we will discuss the apparent dynamic role of ubiquitination in the management of misfolded proteins.KeywordsMisfolded ProteinPolyubiquitin ChainProtein InclusionUbiquitin ChainUbiquitin MoleculeThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves." @default.
- W157037429 created "2016-06-24" @default.
- W157037429 creator A5081705641 @default.
- W157037429 creator A5083225635 @default.
- W157037429 creator A5091427207 @default.
- W157037429 date "2008-12-20" @default.
- W157037429 modified "2023-10-17" @default.
- W157037429 title "Dynamic Role of Ubiquitination in the Management of Misfolded Proteins Associated with Neurodegenerative Diseases" @default.
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