Ontology highlight
ABSTRACT:
SUBMITTER: Tashiro K
PROVIDER: S-EPMC21520 | biostudies-literature | 1997 Jul
REPOSITORIES: biostudies-literature
Tashiro K K Pando M P MP Kanegae Y Y Wamsley P M PM Inoue S S Verma I M IM
Proceedings of the National Academy of Sciences of the United States of America 19970701 15
The NF-kappaB/Rel proteins are sequestered in the cytoplasm in association with IkappaBalpha. In response to external signals, IkappaBalpha is phosphorylated, multi-ubiquitinated, and degraded by proteasomes, thereby releasing NF-kappaB/Rel proteins to migrate to the nucleus. We have cloned a mouse ubiquitin-conjugating enzyme (mE2), which associates with IkappaBalpha. mE2 is homologous to the yeast Ubc9/Hus5 ubiquitin-conjugating enzyme. A transdominant-negative mutant of mE2 had no effect on p ...[more]