IndraLab

"For ataxin-3 to be degraded by the proteasome, it needs to come into contact with this cellular machinery."

"Ataxin-3 is degraded by the proteasome."

"Additionally, when cells were treated with the proteasome inhibitor MG132, more aggregates in the insoluble fraction retained in the FTA filter (Fig 3B), suggesting that proteasome inhibition caused accumulation of ATXN3 polyQ aggregation into HMW fibrils, as observed in Fig 2B and expected from previous studies [30–32]."

"Finally, pulse-chase labeling reveals that ataxin-3 is degraded by the proteasome, with expanded ataxin-3 being as efficiently degraded as normal ataxin-3."

"Wild-type ATXN3 can be degraded by the proteasome, but whether other protein quality control pathways are involved in its turnover remains unknown."

"However, proteasome inhibition triggered polyQ expanded ATXN3 aggregation, a process that could be linked with the global proteostasis collapse induced by this treatment."

"In vitro studies revealed that inactive ataxin-3 was more slowly degraded by the proteasome and that this degradation occurred independent of ubiquitination."

"p45, an ATPase subunit of the 19S proteasome, interacts with ataxin-3 in vitro and stimulates the degradation of ataxin-3 in an in vitro reconstituted degradation assay system."

"Accordingly, as for cytoplasmic aggresomes, proteasome inhibition increases aggregation of ataxin-3 in NBs [57] , and NBs were shown to be proteolysis structures adjacent to proteasomal constituents [[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"The neuroprotective role of HSJ1 has been demonstrated in different disease models : it suppresses the aggregation of polyglutamine expanded proteins, significantly enhancing mutant huntingtin solubility in Huntington disease in cells and in mice, and promoting misfolded protein targeting to the ubiquitin-proteasome system; HSJ1a cooperates with Hsp70 to promote proteasome degradation of ataxin-3, a protein responsible for spinocerebellar ataxia type 3 (SCA3); HSJ1a prevented the aggregation of the misfolded C289G Parkin, a Parkinson disease associated ubiquitin protein ligase mutant, and restored its function in mitophagy."