Ontology highlight
ABSTRACT:
SUBMITTER: Koenig PA
PROVIDER: S-EPMC4263858 | biostudies-other | 2014 Dec
REPOSITORIES: biostudies-other
Koenig Paul-Albert PA Nicholls Peter K PK Schmidt Florian I FI Hagiwara Masatoshi M Maruyama Takeshi T Frydman Galit H GH Watson Nicki N Page David C DC Ploegh Hidde L HL
The Journal of biological chemistry 20141015 50
ER-resident proteins destined for degradation are dislocated into the cytosol by components of the ER quality control machinery for proteasomal degradation. Dislocation substrates are ubiquitylated in the cytosol by E2 ubiquitin-conjugating/E3 ligase complexes. UBE2J1 is one of the well-characterized E2 enzymes that participate in this process. However, the physiological function of Ube2j1 is poorly defined. We find that Ube2j1(-/-) mice have reduced viability and fail to thrive early after birt ...[more]