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Interactions between Autophagy Receptors and Ubiquitin-like Proteins Form the Molecular Basis for Selective Autophagy

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MOLECULAR CELL
卷 53, 期 2, 页码 167-178

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CELL PRESS
DOI: 10.1016/j.molcel.2013.12.014

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Selective autophagy ensures recognition and removal of various cytosolic cargos. Hence, aggregated proteins, damaged organelles, or pathogens are enclosed into the double-membrane vesicle, the autophagosome, and delivered to the lysosome for degradation. This process is mediated by selective autophagy receptors, such as p62/SQSTM1. These proteins recognize autophagic cargo and, via binding to small ubiquitin-like modifiers (UBLs)-Atg8/LC3/GABARAPs and ATG5-mediate formation of selective autophagosomes. Recently, it was found that UBLs can directly engage the autophagosome nucleation machinery. Here, we review recent findings on selective autophagy and propose a model for selective autophagosome formation in close proximity to cargo.

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