Mechanisms for the Selective Degradation of Ubiquitinated Proteins by the 26S Proteasome

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• Fred Goldberg, Harvard Medical School
• Friday 22 June 2012, 16:15-18:00
• Max Perutz Lecture Theatre, Medical Research Council (MRC) (MRC Laboratory of Molecular Biol.

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The 26S Proteasome is the major site for protein degradation in eukaryotic cells and selectively digests proteins marked for degradation by attachment of a ubiquitin chain. Recent studies indicate multiple ATP -dependent steps in this process and clarify how certain types of ubiquitinated proteins become tightly bound and how deubiquitination, ATP hydrolysis, and proteolysis are coupled. In this process, the six proteasomal AAA AT Pase subunits function cooperatively to drive protein unfolding translocation, and opening the gate for substrate-entry into the 20S proteolytic core. Prof Goldberg will also discuss how proteasome function is impaired in certain neurodegenerative disease and the development of the proteasome inhibitors, now widely used as scientific reagents and in the treatment of hematologic cancers.

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

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