Ontology highlight
ABSTRACT:
SUBMITTER: Tam S
PROVIDER: S-EPMC2829982 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Tam Stephen S Geller Ron R Spiess Christoph C Frydman Judith J
Nature cell biology 20060917 10
Misfolding and aggregation of proteins containing expanded polyglutamine repeats underlie Huntington's disease and other neurodegenerative disorders. 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 suffic ...[more]