Ontology highlight
ABSTRACT:
SUBMITTER: Hellerschmied D
PROVIDER: S-EPMC5797217 | biostudies-literature | 2018 Feb
REPOSITORIES: biostudies-literature
Hellerschmied Doris D Roessler Max M Lehner Anita A Gazda Linn L Stejskal Karel K Imre Richard R Mechtler Karl K Dammermann Alexander A Clausen Tim T
Nature communications 20180202 1
Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in vitro and in vivo approach to delineate the substrate-targeting mechanism of UFD-2 and elucidate its distinct mechanistic features as an E3/E4 enzyme. Using Caenorhabditis elegans as model system, we demonstrate that UFD-2 is n ...[more]