Letter abstract


Nature Cell Biology 8, 1155 - 1162 (2006)
Published online: 17 September 2006 | doi:10.1038/ncb1477

The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions

Stephen Tam1,2, Ron Geller2, Christoph Spiess2 & Judith Frydman2


Misfolding and aggregation of proteins containing expanded polyglutamine repeats underlie Huntington's disease and other neurodegenerative disorders1. Here, we show that the hetero-oligomeric chaperonin TRiC (also known as CCT) physically interacts with polyglutamine-expanded variants of huntingtin (Htt) and effectively inhibits their aggregation. Depletion of TRiC enhances polyglutamine aggregation in yeast and mammalian cells. Conversely, overexpression of a single TRiC subunit, CCT1, is sufficient to remodel Htt-aggregate morphology in vivo and in vitro, and reduces Htt-induced toxicity in neuronal cells. Because TRiC acts during de novo protein biogenesis2, this chaperonin may have an early role preventing Htt access to pathogenic conformations. Based on the specificity of the Htt–CCT1 interaction, the CCT1 substrate-binding domain may provide a versatile scaffold for therapeutic inhibitors of neurodegenerative disease.

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  1. Biophysics Graduate Program, Stanford University, Stanford, California 94305, USA.
  2. Department of Biological Sciences, Stanford University, Stanford, California 94305, USA.

Correspondence to: Judith Frydman2 e-mail: jfrydman@stanford.edu



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