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Abstract
Ubiquitination is the hallmark of protein degradation by the 26S proteasome. However,
the proteasome is limited in its capacity to degrade oligomeric and aggregated proteins.
Removal of harmful protein aggregates is mediated by autophagy, a mechanism by which
the cell sequesters cytosolic cargo and delivers it for degradation by the lysosome.
Identification of autophagy receptors, such as p62/SQSTM1 and NBR1, which simultaneously
bind both ubiquitin and autophagy-specific ubiquitin-like modifiers, LC3/GABARAP,
has provided a molecular link between ubiquitination and autophagy. This review explores
the hypothesis that ubiquitin represents a selective degradation signal suitable for
targeting various types of cargo, ranging from protein aggregates to membrane-bound
organelles and microbes.