Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.

Kitamura, Akira; Kubota, Hiroshi; Pack, Chan-Gi; Matsumoto, Gen; Hirayama, Shoshiro; Takahashi, Yasuo; Kimura, Hiroshi; Kinjo, Masataka; Morimoto, Richard; Nagata, Kazuhiro

Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.

Kitamura, Akira; Kubota, Hiroshi; Pack, Chan-Gi et al.

Nature cell biology, 2006, 8(10), 1163-1169

Permalink : https://hdl.handle.net/2115/57990

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アクセス権	open access
URI	https://hdl.handle.net/2115/57990
タイトル	Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.
著者	Kitamura, Akira ; Kubota, Hiroshi ; Pack, Chan-Gi ; Matsumoto, Gen ; Hirayama, Shoshiro ; Takahashi, Yasuo ; Kimura, Hiroshi ; Kinjo, Masataka ; Morimoto, Richard ; Nagata, Kazuhiro
e-Rad_Researcher 10580152 著者名 Kitamura, Akira
e-Rad_Researcher 80332724 著者名 Kubota, Hiroshi
著者名 Pack, Chan-Gi
e-Rad_Researcher 50415303 著者名 Matsumoto, Gen
著者名 Hirayama, Shoshiro
e-Rad_Researcher 90374610 著者名 Takahashi, Yasuo
著者名 Kimura, Hiroshi
e-Rad_Researcher 70177971 著者名 Kinjo, Masataka
著者名 Morimoto, Richard
e-Rad_Researcher 50127114 著者名 Nagata, Kazuhiro
言語	英語
発行日	2006-12
収録物名	Nature cell biology
巻(号)	8(10)
ページ	1163-1169
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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	1465-7392
関連情報	PMID 16980958
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1038/ncb1478