| Literature DB >> 12913066 |
Hitoshi Osaka1, Yu-Lai Wang, Koji Takada, Shuichi Takizawa, Rieko Setsuie, Hang Li, Yae Sato, Kaori Nishikawa, Ying-Jie Sun, Mikako Sakurai, Takayuki Harada, Yoko Hara, Ichiro Kimura, Shigeru Chiba, Kazuhiko Namikawa, Hiroshi Kiyama, Mami Noda, Shunsuke Aoki, Keiji Wada.
Abstract
Mammalian neuronal cells abundantly express a deubiquitylating enzyme, ubiquitin carboxy-terminal hydrolase 1 (UCH L1). Mutations in UCH L1 are linked to Parkinson's disease as well as gracile axonal dystrophy (gad) in mice. In contrast to the UCH L3 isozyme that is universally expressed in all tissues, UCH L1 is expressed exclusively in neurons and testis/ovary. We found that UCH L1 associates and colocalizes with monoubiquitin and elongates ubiquitin half-life. The gad mouse, in which the function of UCH L1 is lost, exhibited a reduced level of monoubiquitin in neurons. In contrast, overexpression of UCH L1 caused an increase in the level of ubiquitin in both cultured cells and mice. These data suggest that UCH L1, with avidity and affinity for ubiquitin, insures ubiquitin stability within neurons. This study is the first to show the function of UCH L1 in vivo.Entities:
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Year: 2003 PMID： 12913066 DOI： 10.1093/hmg/ddg211
Source DB: PubMed Journal: Hum Mol Genet ISSN： 0964-6906 Impact factor: 6.150