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Yuu Miyauchi Last modified date:2020.02.14

Assistant Professor / Division of Pharmaceutical Cell Biology
Department of Pharmaceutical Health Care and Sciences
Faculty of Pharmaceutical Sciences

Graduate School
Undergraduate School

Academic Degree
Ph.D. (Pharmaceutical Sciences)
Field of Specialization
Drug Metabolism
Research Interests
  • Analysis of effects of protein-protein interaction and subcellular localization of drug metabolizing enzymes on thier catalytic activities
    keyword : Drug metabolism, Targeting to the ER membrane, protein-protien interaction, subcellular localization
Academic Activities
1. Yuu Miyauchi, Sora Kimura, Akane Kimura, Ken Kurohara, Yuko Hirota, Keiko Fujimoto, Peter I. Mackenzie, Yoshitaka Tanaka, Yuji Ishii, Investigation of the endoplasmic reticulum localization of UDP-glucuronosyltransferase 2B7 with systematic deletion mutants, Molecular Pharmacology, 10.1124/mol.118.113902, 95, 5, 551-562, 2019.05, UDP-Glucuronosyltransferase (UGT) plays an important role in the metabolism of endogenous and exogenous compounds. UGT is a type I membrane protein, and has a dilysine motif (KKXX/KXKXX) in its C-terminal cytoplasmic domain. Although a dilysine motif is defined as an endoplasmic reticulum (ER) retrieval signal, it remains a matter of debate whether this motif functions in the ER localization of UGT. To address this issue, we generated systematic deletion mutants of UGT2B7, a major human isoform, and compared their subcellular localizations with that of an ER marker protein calnexin (CNX), using subcellular fractionation and immunofluorescent microscopy. We found that although the dilysine motif functioned as the ER retention signal in a chimera that replaced the cytoplasmic domain of CD4 with that of UGT2B7, UGT2B7 truncated mutants lacking this motif extensively colocalized with CNX, indicating dilysine motif–independent ER retention of UGT2B7. Moreover, deletion of the C-terminal transmembrane and cytoplasmic domains did not affect ER localization of UGT2B7, suggesting that the signal necessary for ER retention of UGT2B7 is present in its luminal domain. Serial deletions of the luminal domain, however, did not affect the ER retention of the mutants. Further, a cytoplasmic and transmembrane domain–deleted mutant of UGT2B7 was localized to the ER without being secreted. These results suggest that UGT2B7 could localize to the ER without any retention signal, and lead to the conclusion that the static localization of UGT results from lack of a signal for export from the ER..
2. Yuu Miyauchi, Kiyoshi Nagata, Yasushi Yamazoe, Peter I. Mackenzie, Yamada, H., YUJI ISHII, Suppression of cytochrome P450 3A4 function by UDP-glucuronosyltransferase 2B7 through a protein-protein interaction: cooperative roles of the cytosolic carboxyl-terminal domain and the luminal anchoring region, Mol. Pharmacol., 88, 800-812, 2015.10.
1. @Miyauchi Y., Tanaka Y., Nagata K., Yamazoe Y., Mackenzie P.I., and Ishii Y. , Effect of dexamethasone treatment on cytochrome P450 3A-UDP-glucuronosyltransferase 1A interaction in rat liver, 12th International ISSX Meeting, 2019.07.
2. Yuu Miyauchi, YUJI ISHII, Kiyoshi Nagata, Yasushi Yamazoe, Peter I. Mackenzie, Yamada, H., Suppression of cytochrome P450 3A4 activity by UDP-glucuronosyltransferase (UGT) 2B7: the role of charged residue(s) in the cytosolic tail of UGT2B7, 19th North American ISSX and 29th JSSX, 2014.10.
Membership in Academic Society
  • International Society for the Study of Xenobiotics
  • The Japanese Society of Toxicology
  • The Japanese Society for the Study of Xenobiotics
  • the Pharmaceutical Society of Japan