TL;DR
Findings identify USP28 as a proteostasis-associated deubiquitinase reduced in HD models and suggest that USP28 deficiency contributes to ubiquitin burden and mHTT aggregation.
Huntington’s disease (HD) is a neurodegenerative disorder caused by abnormal expansions of poly-glutamine repeats in the mutant Huntingtin (mHTT). The expanded proteins form pathological aggregates to disrupt neuronal functions during disease progression, suggesting the clearance of the aggregates is considered as a po...
Huntington's disease (HD) offers a particularly instructive, if sobering, window into what happens when a cell's protein-clearance machinery is asked to do more than it can bear. Background: the ubiquitin-proteasome system (UPS) is the principal route by which short-lived and misfolded proteins are removed from eukaryo...
It is demonstrated that G3BP1 also stabilises the COPI vesicle protein beta-COP by promoting its interaction with the deubiquitinase USP10, which accelerates its proteasomal degradation.
The RNA-binding protein YTHDC1 is identified as an ATP-independent molecular chaperone that prevents harmful protein aggregation, revealing a link between RNA regulation and protein quality control in neurodegeneration.
Amyotrophic lateral sclerosis is a fatal neurodegenerative disease characterized by the cytoplasmic mislocalization, aberrant phosphorylation and pathological aggregation of TDP-43, a nuclear RNA-binding protein essential for RNA metabolism. Despite its central involvement in ALS pathogenesis, the molecular mechanisms...
Bcl-2-associated athanogene 3 (BAG3) is a mediator of chaperone-assisted selective autophagy, and in the brain, is most highly expressed in astrocytes. However, its role in astrocytes remains poorly defined. Given the genetic and pathological links of BAG3 to proteostasis and neurodegenerative diseases, we investigated...
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