TY  - GEN
T1  - Chemical mutagenesis of Caenorhabditis elegans uncovers genetic modifiers of huntingtin protein aggregation
AU  - Ung, Hailey M
AU  - Hall, Rhodes H
AU  - Kikis, Elise A
DO  - 10.17912/micropub.biology.000202
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000202/
AB  - Huntington’s disease (HD) is an autosomal dominant monogenic neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the protein huntingtin (Htt) (MacDonald et al., 1993). The resultant disease-associated Htt protein harbors a polyglutamine (polyQ) repeat that renders it metastable with respect to folding (Carrell and Lomas, 1997). Htt protein misfolding, characterized by the accumulation of misfolded protein aggregates and neurotoxicity, is first observed in mid- to late-life for most HD patients (Becher et al., 1998). The age-of-onset for HD is inversely proportional to CAG repeat length (Becher et al., 1998). Nonetheless, genetic variation between HD patients is attributed to slight differences in age-of-onset, even when repeat length is the same (Gusella and MacDonald, 2000). Thus, genetic background seems to be an important modifier of Htt protein aggregation and toxicity. We are interested in identifying genes/proteins that enhance or suppress the folding defect of human Htt.
PY  - 2020
JO  - microPublication Biology
ER  -