Oxford Events, the new replacement for OxTalks, will launch on 16th March. From now until the launch of Oxford Events, new events cannot be published or edited on OxTalks while all existing records are migrated to the new platform. The existing OxTalks site will remain available to view during this period.
From 16th, Oxford Events will launch on a new website: events.ox.ac.uk, and event submissions will resume. You will need a Halo login to submit events. Full details are available on the Staff Gateway.
The long-term health of cells critically relies on selective protein degradation since damaged or aggregated proteins cause proteotoxic stress that can impair cell function and cause cell death. Many neuro-degenerative diseases, including Alzheimer’s, Parkinson’s, Huntington’s Disease, ALS and retinitis pigmentosa, are caused by the accumulation of protein aggregates. We recently discovered a novel mechanism that enables cells to avoid proteotoxic stress by stimulating the assembly of proteasomes, the multi-protein protease complex responsible for the regulated proteolysis of intracellular proteins. Significantly, this pathway is sensitive to diet, mitochondrial function, and oxidative stress. Furthermore, the activity of this pathway declines with age. Finally, polymorphisms in the central factor in this pathway, PI31, are associated factor with Alzheimer’s Disease. Our findings suggest that insufficient availability of proteasomes contributes to the aging process and chronic neuro-degenerative diseases.
Background reading:
Bader, M. Benjamin, S. Wapinski O., Smith, DM., Goldberg, AL., and Steller, H. (2011). A conserved F-box-regulatory complex controls proteasome activity in Drosophila. Cell. 145, 371-82.
Cho-Park, P., and Steller, H. (2013). Proteasome regulation by ADP-ribosylation. Cell, 153, 614–627.
