Misfolded proteins partition between two distinct quality control compartments

By Daniel Kaganovich, R. Kopito, Judith Frydman. Nature, 2008

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Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans (2010, background): “Chaperones and the proteasome play a major role in preventing the accumulation of misfolded proteins and are directly implicated in preventing protein aggregation [13,74,75,76].”
Cellular strategies for controlling protein aggregation (2010, background): “Organizing protein aggregates might also facilitate the efficiency of aggregate removal in a subsequent phas”
p62 links the autophagy pathway and the ubiqutin–proteasome system upon ubiquitinated protein degradation (2016, neutral): “different pattern compared with the misfolded protein upon proteasome inhibition [83], i.”
Molecular chaperones in protein folding and proteostasis (2011, background): “Interestingly, whereas the clearance of misfolded protein species by the UPS requires that these molecules are maintained in a non-aggregated state by chaperones, disposal by autophagy is thought to involve active mechanisms to force such molecules into larger, presumably less toxic, aggregate”
In vivo aspects of protein folding and quality control (2016, background): “Interestingly, recent evidence indicates that cells contain machineries that actively sequester surplus and misfolded proteins into transient or stable deposits when their timely degradation fails (161-168), presumably an attempt to reduce toxic effects exerted by soluble oligomers (169).”