Ontology highlight
ABSTRACT:
SUBMITTER: Shmueli A
PROVIDER: S-EPMC3014991 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Shmueli Ayelet A Tsai Yien Che YC Yang Mei M Braun Mary A MA Weissman Allan M AM
Biochemical and biophysical research communications 20091014 3
There are an increasing number of ubiquitin ligases (E3s) implicated in endoplasmic reticulum (ER)-associated degradation (ERAD) in mammals. The two for which the greatest amount of information exists are the RING finger proteins gp78 and Hrd1, which are the structural orthologs of the yeast ERAD E3 Hrd1p. We now report that Hrd1, also known as synoviolin, targets gp78 for proteasomal degradation independent of the ubiquitin ligase activity of gp78, without evidence of a reciprocal effect. This ...[more]