Ontology highlight
ABSTRACT:
SUBMITTER: Chen M
PROVIDER: S-EPMC3107271 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Chen Meifan M Gutierrez Gustavo J GJ Ronai Ze'ev A ZA
Proceedings of the National Academy of Sciences of the United States of America 20110513 22
The ubiquitin-recognition protein Ufd1 facilitates clearance of misfolded proteins through the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Here we report that prolonged ER stress represses Ufd1 expression to trigger cell cycle delay, which contributes to ERAD. Remarkably, down-regulation of Ufd1 enhances ubiquitination and destabilization of Skp2 mediated by the anaphase-promoting complex or cyclosome bound to Cdh1 (APC/C(Cdh1)), resulting in accumulation of the cyclin-depe ...[more]