Regulation of proteasome function in normal and disease states

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• Professor Alfred Goldberg, Harvard Medical School
• Friday 15 May 2015, 16:15-17:15
• Max Perutz Lecture Theatre, Medical Research Council (MRC) (MRC Laboratory of Molecular Biol.

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Synopsis: It is generally assumed that degradation by the ubiquitin-proteasome pathway is regulated solely by ubiquitination. However, we recently found several novel cellular mechanism that regulate proteasome content and functional capacity. When proteasomes are inhibited pharmacologically or become stalled, they have a mechanism that prevents further binding of ubiquitin conjugates, and they stimulate production of new proteasomes by enhancing transcription of genes for all proteasome subunits. We also have found that proteasome capacity to degrade ubiquitin conjugates and misfolded aggregation-prone proteins in cells is enhanced by phosphorylation of a 19S regulatory subunit. In certain mouse or cellular models of neurodegenerative disease, the 26S proteasome’s capacity to degrade ubiquitinated proteins is impaired, but can be activated by pharmacological agents that promote proteasome phosphorylation and thus enhance the degradation of the toxic proteins.

This talk is part of the MRC LMB Seminar Series series.

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