Kyushu University Academic Staff Educational and Research Activities Database
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Yuu Miyauchi Last modified date:2019.03.29

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. Saki Gotoh, Yuu Miyauchi, Rick Moore, Masahiko Negishi, Glucose elicits serine/threonine kinase VRK1 to phosphorylate nuclear pregnane X receptor as a novel hepatic gluconeogenic signal, Cellular Signalling, 10.1016/j.cellsig.2017.09.003, 40, 200-209, 2017.12, Low glucose stimulated phosphorylation of pregnane X receptor (PXR) at Ser350 in correlation with an increased gluconeogenesis in human hepatoma-derived HepG2 cells. Only glucose, but neither insulin nor glucagon, stimulated this phosphorylation. Here, serine/threonine kinase, vaccinia related kinase 1 (VRK1)-mediated phosphorylation of PXR is now defined as this glucose-elicited novel signal. In low glucose conditions, VRK1 directly phosphorylates PXR at Ser350, enabling PO3-PXR to scaffold protein phosphatase PP2Cα. This PP2Cα dephosphorylates serine/threonine kinase 2 (SGK2) at Thr193. This dephosphorylation dissociates SGK2 from and actives the phosphoenolpyruvate carboxykinase 1 (PCK1) gene as phosphorylated SGK2 binds and represses the gene. Conversely, VRK1 self-represses its activity to phosphorylate PXR through cyclin-dependent kinase 2 (CDK2) in high glucose conditions, resulting in the repression of the PCK1 gene. This PXR phosphorylation was also observed in fasting mouse livers. Thus, the VRK1-CDK2-PXR-PP2Cα-SGK2 pathway can be a novel physiological cell signaling that regulates gluconeogenesis in response to glucose..
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. Yuu Miyauchi, YUJI ISHII, Yamada, H., Alteration of Cytochrome P450 Activity by UDP-Glucuronosyltransferase 2B7, 4th Asian Pacific Regional Meeting of ISSX, 2011.04.
2. Yuu Miyauchi, YUJI ISHII, Kiyoshi Nagata, Yasushi Yamazoe, Peter I. Mackenzie, Yamada, H., UDP-Glucuronosyltransferase (UGT) 2B7 and 1A9 suppress cytochrome P450 function: evidence for the involvement of the cytosolic tail of UGT in the suppression, 19th MDO and 12th European ISSX, 2012.06.
3. 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.
4. Yuu Miyauchi, Saki Gotoh, Rick Moore, Masahiko Negishi, PXR transduces glucose signal to regulate hepatic metabolism via phosphorylation at Ser350, 21st International Symposium on Microsomes and Drug Oxidations, 2016.10.
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