Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation.

ABSTRACT: Protein misfolding and the formation of aggregates are increasingly recognized components of the pathology of human genetic disease and hallmarks of many neurodegenerative disorders. As exemplified by polyglutamine diseases, the propensity for protein misfolding is associated with the length of polyglutamine expansions and age-dependent changes in protein-folding homeostasis, suggesting a critical role for a protein homeostatic buffer. To identify the complement of protein factors that protects cells against the formation of protein aggregates, we tested transgenic Caenorhabditis elegans strains expressing polyglutamine expansion yellow fluorescent protein fusion proteins at the threshold length associated with the age-dependent appearance of protein aggregation. We used genome-wide RNA in

SUBMITTER: Nollen EA 

PROVIDER: S-EPMC404057 | biostudies-literature | 2004 Apr

REPOSITORIES: biostudies-literature