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Protein degradation and defense against neurodegenerative disease 2

Part 2 of 2
Published on October 7, 2014   42 min

A selection of talks on Neurology

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0:04
In this lecture, I want to focus on the functioning of the 26S proteasome. This has been an exciting area of recent research and is of increasing importance in our understanding of neurodegenerative disease and biology, generally. This side illustrates the major components of the ubiquitin proteasome pathway using the cryo-EM, single particle EM, from the laboratory of Wolfgang Baumeister in Munich. Proteins are actually degraded within the core 20S proteasome shown here in yellow. The degradation occurs within a very tight protein coat. Shown by the scissors, there are six active sites that cleave after hydrophobic, basic or acidic residues in an isolated compartment away from the cytosol. However, for proteins to be injected into the core 20S proteasome, they have to be generally ubiquitinated and bind to the 19S regulatory complex shown here in blue. This has the receptors for the ubiquitin chain and also contains six ATP-hydrolyzing sub units that carry out the unfolding of substrates and their translocation into the 20S proteasome for degradation. And we are now able to explain these processes at near-molecular understanding. They also have important relevance to human disease which I'd like to discuss.
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Protein degradation and defense against neurodegenerative disease 2

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