Ontology highlight
ABSTRACT:
SUBMITTER: Yonashiro R
PROVIDER: S-EPMC1538564 | biostudies-literature | 2006 Aug
REPOSITORIES: biostudies-literature
Yonashiro Ryo R Ishido Satoshi S Kyo Shinkou S Fukuda Toshifumi T Goto Eiji E Matsuki Yohei Y Ohmura-Hoshino Mari M Sada Kiyonao K Hotta Hak H Yamamura Hirohei H Inatome Ryoko R Yanagi Shigeru S
The EMBO journal 20060727 15
In this study, we have identified a novel mitochondrial ubiquitin ligase, designated MITOL, which is localized in the mitochondrial outer membrane. MITOL possesses a Plant Homeo-Domain (PHD) motif responsible for E3 ubiquitin ligase activity and predicted four-transmembrane domains. MITOL displayed a rapid degradation by autoubiquitination activity in a PHD-dependent manner. HeLa cells stably expressing a MITOL mutant lacking ubiquitin ligase activity or MITOL-deficient cells by small interferin ...[more]