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How ER Stress Pathways Affect the Trafficking and Degradation of Protein Aggregates
LYSOSOME SHIFTING BY THE UNFOLDED PROTEIN RESPONSE
Julie Hollien, Danny Bae, Rachel Jones, Katie Piscopo
University of Utah, Salt Lake City, UT, USA
We've found that stress in the endoplasmic reticulum leads to the activation of an mRNA decay pathway specific for ER-localized mRNAs. Degradation of a single target of this pathway, Blos1, initiates a cascade of events that repositions organelles of the endomembrane system and allows for more effective clearance of protein aggregates. Surprisingly, the degradation of aggregating proteins prior to the formation of large juxtanuclear aggregates appears to involve encapsulation into late endosomes via the ESCRT-dependent multivesicular body pathway. I will discuss the mechanisms underlying this pathway, and how this helps cells deal with pathological protein aggregates that accumulate during Huntington's disease.
This work was supported by an NIH MIRA (R35 GM119540).
Speakers
Julie Hollien