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Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.

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Title: Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.
Authors: Kitamura, Akira Browse this author →KAKEN DB
Kubota, Hiroshi Browse this author →KAKEN DB
Pack, Chan-Gi Browse this author
Matsumoto, Gen Browse this author →KAKEN DB
Hirayama, Shoshiro Browse this author
Takahashi, Yasuo Browse this author →KAKEN DB
Kimura, Hiroshi Browse this author
Kinjo, Masataka Browse this author →KAKEN DB
Morimoto, Richard Browse this author
Nagata, Kazuhiro Browse this author →KAKEN DB
Issue Date: Dec-2006
Journal Title: Nature cell biology
Volume: 8
Issue: 10
Start Page: 1163
End Page: 1169
Publisher DOI: 10.1038/ncb1478
PMID: 16980958
Abstract: 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.
Type: article (author version)
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 北村 朗

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