Ontology highlight
ABSTRACT:
SUBMITTER: Hjerpe R
PROVIDER: S-EPMC5003816 | biostudies-other | 2016 Aug
REPOSITORIES: biostudies-other
Cell 20160728 4
Clearance of misfolded and aggregated proteins is central to cell survival. Here, we describe a new pathway for maintaining protein homeostasis mediated by the proteasome shuttle factor UBQLN2. The 26S proteasome degrades polyubiquitylated substrates by recognizing them through stoichiometrically bound ubiquitin receptors, but substrates are also delivered by reversibly bound shuttles. We aimed to determine why these parallel delivery mechanisms exist and found that UBQLN2 acts with the HSP70-HS ...[more]