Kyushu University Academic Staff Educational and Research Activities Database
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Yuta Amagai Last modified date:2024.05.01





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Phone
092-642-6833
Academic Degree
Ph.D. (Life sciences)
Country of degree conferring institution (Overseas)
No
Field of Specialization
Cell biology, Biochemistry
ORCID(Open Researcher and Contributor ID)
0000-0002-2999-4622
Total Priod of education and research career in the foreign country
00years00months
Research
Research Interests
  • Molecular mechanisms of the regulation of zinc homeostasis in the early secretory pathway mediated by zinc transporters
    keyword : zinc transporter, endoplasmic reticulum, Golgi apparatus, zinc
    2019.04.
  • Molecular mechanisms of the regulation of ERp44 in the early secretory pathway
    keyword : ERp44, endoplasmic reticulum, Golgi apparatus, pH, zinc
    2015.04.
Academic Activities
Papers
1. Yuta Amagai, Momo Yamada, Toshiyuki Kowada, Tomomi Watanabe, Yuyin Du, Rong Liu, Satoshi Naramoto, Satoshi Watanabe, Junko Kyozuka, Tiziana Anelli, Tiziana Tempio, Roberto Sitia, Shin Mizukami, Kenji Inaba, Zinc homeostasis governed by Golgi-resident ZnT family members regulates ERp44-mediated proteostasis at the ER-Golgi interface, Nature Communications, 10.1038/s41467-023-38397-6, 14, 1, 2683-2683, 2023.05, Many secretory enzymes acquire essential zinc ions (Zn2+) in the Golgi complex. ERp44, a chaperone operating in the early secretory pathway, also binds Zn2+ to regulate its client binding and release for the control of protein traffic and homeostasis. Notably, three membrane transporter complexes, ZnT4, ZnT5/ZnT6 and ZnT7, import Zn2+ into the Golgi lumen in exchange with protons. To identify their specific roles, we here perform quantitative Zn2+ imaging using super-resolution microscopy and Zn2+-probes targeted in specific Golgi subregions. Systematic ZnT-knockdowns reveal that ZnT4, ZnT5/ZnT6 and ZnT7 regulate labile Zn2+ concentration at the distal, medial, and proximal Golgi, respectively, consistent with their localization. Time-course imaging of cells undergoing synchronized secretory protein traffic and functional assays demonstrates that ZnT-mediated Zn2+ fluxes tune the localization, trafficking, and client-retrieval activity of ERp44. Altogether, this study provides deep mechanistic insights into how ZnTs control Zn2+ homeostasis and ERp44-mediated proteostasis along the early secretory pathway..
Membership in Academic Society
  • The molecular biology society of Japan
Awards
  • Metallomics Poster Prize