Specific types of ubiquitin chains function as molecular signals for clearance and quality control of damaged mitochondria. USP30 regulates the level of ubiquitin chains on mitochondria by selectively cleaving them. We elucidated the mechanism of this ubiquitin chain cleavage by USP30 at the atomic level. Our findings will lead to the development of therapeutic drugs against Parkinson’s disease. This study was carried out in collaboration with Keiji Tanaka and his colleagues. (Tokyo Metropolitan Institute of Medical Science)
JST CREST （http://www.jst.go.jp/kisoken/crest/en/）
Research Area “Structural Life Science and Advanced Core Technologies for Innovative Life Science Research”
Research Theme “Structural life science of membrane receptor complexes and their downstream signaling for synapse formation”
Yusuke Sato, Kei Okatsu, Yasushi Saeki, Koji Yamano, Noriyuki Matsuda, Ai Kaiho, Atsushi Yamagata, Sakurako Goto-Ito, Minoru Ishikawa, Yuichi Hashimoto, Keiji Tanaka and Shuya Fukai. “Structural basis for specific cleavage of Lys6-linked polyubiquitin chains by USP30”, Nature Structural & Molecular Biology, published online Sep. 26, 2017, doi: 10.1038/nsmb.3469.
Shuya Fukai, D.Sc.,
Associate Professor, Institute of Molecular and Cellular Biosciences, The University of Tokyo
Life Innovation Group, Department of Innovation Research, JST