Ontology highlight
ABSTRACT:
SUBMITTER: Yang H
PROVIDER: S-EPMC5377324 | biostudies-literature | 2014 Sep
REPOSITORIES: biostudies-literature
Yang Hui H Li Jing-Jing JJ Liu Shuai S Zhao Jian J Jiang Ya-Jun YJ Song Ai-Xin AX Hu Hong-Yu HY
Scientific reports 20140918
Expansion of polyglutamine (polyQ) tract may cause protein misfolding and aggregation that lead to cytotoxicity and neurodegeneration, but the underlying mechanism remains to be elucidated. We applied ataxin-3 (Atx3), a polyQ tract-containing protein, as a model to study sequestration of normal cellular proteins. We found that the aggregates formed by polyQ-expanded Atx3 sequester its interacting partners, such as P97/VCP and ubiquitin conjugates, into the protein inclusions through specific int ...[more]