CAS NE 525 Lecture Notes - Lecture 5: Mitophagy, Heavy Metals, Subthalamic Nucleus
10 Aug 2018
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Document Summary
Ubiquitin proteasome pathway: mechanism that uses addition of ubiquitin chain as a tag/signal for proteins that need to be degraded. Brought to proteasome for catalytic activity which degrades the proteins. Two major steps: substrate (protein that needs to be degraded: deconjugation: activation of proteins which are enzymes that activate ubiquitin (modify it from a biochemical perspective). So it can be transferred to protein substrates that need to be degraded by ubiquitin transferases/ligases, ubiquitin ___ (e1, e2, e3): conjugation: substrate is bound with chain of ubiquitin residues. Substrate transferred to proteasome where degradation of misfolded protein (substrate) happens. Barrel structure made of regulatory particles (contains atpase active sties) and core particles (contain protease active site) Many ways molecules can make it to lysosomes. Transmembrane proteins can be bound by ubiquitin, they form into mvbs (multivesicular bodies), membrane fusion happens then they are eaten by lysosome. Autophagy: method to control the degradation of proteins, organelles, structure, and aggregates through lysosomal pathway.
