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Fig. 2. Autophagic inhibition can impair proteasomal flux, leading to the accumulation of ubiquitinated substrates and their aggregates. In this model, autophagic inhibition causes the accumulation of misfolded proteins and aggregates associated with p62 aggregates, which, in turn, sequester ubiquitinated substrates from the UPS machinery and the regulators of the UPS, such as p97/VCP. In addition, autophagy inhibition can impair the autophagic degradation of the proteasome, leading to the accumulation of aging or damaged proteasomes at the expense of healthy and normal proteasomes.
Mol. Cells 2017;40:441~449
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