Ontology highlight
ABSTRACT:
SUBMITTER: Zaffagnini G
PROVIDER: S-EPMC5830917 | biostudies-literature | 2018 Mar
REPOSITORIES: biostudies-literature
Zaffagnini Gabriele G Savova Adriana A Danieli Alberto A Romanov Julia J Tremel Shirley S Ebner Michael M Peterbauer Thomas T Sztacho Martin M Trapannone Riccardo R Tarafder Abul K AK Sachse Carsten C Martens Sascha S
The EMBO journal 20180117 5
The removal of misfolded, ubiquitinated proteins is an essential part of the protein quality control. The ubiquitin-proteasome system (UPS) and autophagy are two interconnected pathways that mediate the degradation of such proteins. During autophagy, ubiquitinated proteins are clustered in a p62-dependent manner and are subsequently engulfed by autophagosomes. However, the nature of the protein substrates targeted for autophagy is unclear. Here, we developed a reconstituted system using purified ...[more]