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Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.

NCB_Final_Kitamura_MS.pdf12.41 MBPDF見る/開く

タイトル: Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.
著者: Kitamura, Akira 著作を一覧する
Kubota, Hiroshi 著作を一覧する
Pack, Chan-Gi 著作を一覧する
Matsumoto, Gen 著作を一覧する
Hirayama, Shoshiro 著作を一覧する
Takahashi, Yasuo 著作を一覧する
Kimura, Hiroshi 著作を一覧する
Kinjo, Masataka 著作を一覧する
Morimoto, Richard 著作を一覧する
Nagata, Kazuhiro 著作を一覧する
発行日: 2006年12月
誌名: Nature cell biology
巻: 8
号: 10
開始ページ: 1163
終了ページ: 1169
出版社 DOI: 10.1038/ncb1478
抄録: Polyglutamine (polyQ)-expansion proteins cause neurodegenerative disorders including Huntington's disease, Kennedy's disease and various ataxias. The cytotoxicity of these proteins is associated with the formation of aggregates or other conformationally toxic species. Here, we show that the cytosolic chaperonin CCT (also known as TRiC) can alter the course of aggregation and cytotoxicity of huntingtin (Htt)-polyQ proteins in mammalian cells. Disruption of the CCT complex by RNAi-mediated knockdown enhanced Htt-polyQ aggregate formation and cellular toxicity. Analysis of the aggregation states of the Htt-polyQ proteins by fluorescence correlation spectroscopy revealed that CCT depletion results in the appearance of soluble Htt-polyQ aggregates. Similarly, overexpression of all eight subunits of CCT suppressed Htt aggregation and neuronal cell death. These results indicate that CCT has an essential role in protecting against the cytotoxicity of polyQ proteins by affecting the course of aggregation.
資料タイプ: article (author version)
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 北村 朗


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