Dynamic Role of Ubiquitination in the Management of Misfolded Proteins Associated with Neurodegenerative Diseases
作者： Esther S. P. Wong , Jeanne M. M. Tan , Kah-Leong Lim
DOI: 10.1007/978-1-4020-9434-7_3
关键词:
摘要: Protein aggregation as a result of misfolding is common theme underlying neurodegenerative diseases. Although subject intense research, how misfolded proteins bypass sophisticated protein quality control measures in the cell to be deposited 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 proteolytic stress, may switch non-proteolytic form ubiquitination help divert away from an overloaded proteasome. In way, preserve its function over prolonged periods stress and recover thereafter. Supporting this, we recently found lysine (K) 63-linked ubiquitin modification promotes formation inclusions associated with several major Importantly, further K63-linked polyubiquitin selectively facilitates subsequent clearance via autophagy. chapter, will discuss apparent dynamic role management proteins.
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