Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron

Hitoshi Osaka, 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

研究成果: ジャーナルへの寄稿学術誌査読

318 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)1945-1958
ページ数14
ジャーナルHuman molecular genetics
12
16
DOI
出版ステータス出版済み - 8月 15 2003

!!!All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 遺伝学
  • 遺伝学(臨床)

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