Ontology highlight
ABSTRACT:
SUBMITTER: Schmidt CC
PROVIDER: S-EPMC7319771 | biostudies-literature | 2020 Jun
REPOSITORIES: biostudies-literature
Schmidt Claudia C CC Vasic Vedran V Stein Alexander A
eLife 20200626
In endoplasmic reticulum-associated protein degradation (ERAD), membrane proteins are ubiquitinated, extracted from the membrane, and degraded by the proteasome. The cytosolic ATPase Cdc48 drives extraction by pulling on polyubiquitinated substrates. How hydrophobic transmembrane (TM) segments are moved from the phospholipid bilayer into cytosol, often together with hydrophilic and folded ER luminal protein parts, is not known. Using a reconstituted system with purified proteins from <i>Saccharo ...[more]