Ontology highlight
ABSTRACT:
SUBMITTER: Itakura E
PROVIDER: S-EPMC4942676 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Itakura Eisuke E Zavodszky Eszter E Shao Sichen S Wohlever Matthew L ML Keenan Robert J RJ Hegde Ramanujan S RS
Molecular cell 20160623 1
We investigated how mitochondrial membrane proteins remain soluble in the cytosol until their delivery to mitochondria or degradation at the proteasome. We show that Ubiquilin family proteins bind transmembrane domains in the cytosol to prevent aggregation and temporarily allow opportunities for membrane targeting. Over time, Ubiquilins recruit an E3 ligase to ubiquitinate bound clients. The attached ubiquitin engages Ubiquilin's UBA domain, normally bound to an intramolecular UBL domain, and st ...[more]