P62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome.

ABSTRACT: The ubiquitin-proteasome system and autophagy are the two main proteolytic systems involved in, among other functions, the maintenance of cell integrity by eliminating misfolded and damaged proteins and organelles. Both systems remove their targets after their conjugation with ubiquitin. An interesting, yet incompletely understood problem relates to the fate of the components of the two systems. Here we provide evidence that amino acid starvation enhances polyubiquitination on specific sites of the proteasome, a modification essential for its targeting to the autophagic machinery. The uptake of the ubiquitinated proteasome is mediated by its interaction with the ubiquitin-associated domain of p62/SQSTM1, a process that also requires interaction with LC3. Importantly, deletion of the PB1 do

SUBMITTER: Cohen-Kaplan V 

PROVIDER: S-EPMC5127335 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature