IndraLab
Statements
reach
"As the Ubp8 ortholog USP22 was recently shown to interact with, deubiquitinate, and stabilize the Sir2 ortholog Sirt1, and conversely Sirt1 has been shown to mediate deacetylation of USP22 and the SAGA coactivator complex, the discovery of genetic and functional relationships between Sgf73, Ubp8, and Sir2 in yeast strongly suggests that mutant ataxin-7 protein could be impairing the function of not only Gcn5 in the context of the STAGA complex, but also USP22 in the deubiquitinase module."
reach
"While the role of altered STAGA and USP22 deubiquitination complex function in SCA7 disease pathogenesis is unclear, recent studies of the related polyQ disorder SCA1 indicate that the polyQ expansion in ataxin-1 attenuates the formation and function of the Capicua transcription factor complex, contributing to SCA1 disease pathogenesis through a partial loss-of-function mechanism."