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A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics.


ABSTRACT: 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 interfering RNA showed an aberrant mitochondrial morphology such as fragmentation, suggesting the enhancement of mitochondrial fission by MITOL dysfunction. Indeed, a dominant-negative expression of Drp1 mutant blocked mitochondrial fragmentation induced by MITOL depletion. We found that MITOL associated with and ubiquitinated mitochondrial fission protein hFis1 and Drp1. Pulse-chase experiment showed that MITOL overexpression increased turnover of these fission proteins. In addition, overexpression phenotype of hFis1 could be reverted by MITOL co-overexpression. Our finding indicates that MITOL plays a critical role in mitochondrial dynamics through the control of mitochondrial fission proteins.

SUBMITTER: Yonashiro R 

PROVIDER: S-EPMC1538564 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature

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A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics.

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]

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