Article
FUS/TLS acts as an aggregation-dependent modifier of polyglutamine disease model mice.
Scientific reports - 14 Oct 2016
Kino Yoshihiro, Washizu Chika, Kurosawa Masaru, Yamada Mizuki, Doi Hiroshi, Takumi Toru, Adachi Hiroaki, Katsuno Masahisa, Sobue Gen, Hicks Geoffrey G, Hattori Nobutaka, Shimogori Tomomi, Nukina Nobuyuki
Abstract excerpt
FUS/TLS is an RNA/DNA-binding protein associated with neurodegenerative diseases including amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Previously, we found that a prion-like domain in the N-terminus of FUS/TLS mediates co-aggregation between FUS/TLS and mutant huntingtin, the gene product of Huntington's disease (HD). Here, we show that heterozygous knockout of FUS/TLS worsened the...
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