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Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn²⁺ uptake into the Golgi apparatus
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- Bui, Han Ba
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University; Department of Molecular and Chemical Life Sciences, Graduate School of Life Sciences, Tohoku University
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- Watanabe, Satoshi
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University; Department of Molecular and Chemical Life Sciences, Graduate School of Life Sciences, Tohoku University; epartment of Chemistry, Graduate School of Science, Tohoku University
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- Nomura, Norimichi
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
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- Liu, Kehong
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
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- Uemura, Tomoko
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
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- Inoue, Michio
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
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- Tsutsumi, Akihisa
- Graduate School of Medicine, The University of Tokyo
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- Fujita, Hiroyuki
- Advanced Research Laboratory, Canon Medical Systems Corporation
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- Kinoshita, Kengo
- Department of System Bioinformatics, Graduate School of Information Sciences, Tohoku University; Department of Integrative Genomics, Tohoku Medical Megabank Organization, Tohoku University
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- Kato, Yukinari
- Graduate School of Medicine, Tohoku University
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- Iwata, So
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
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- Kikkawa, Masahide
- Graduate School of Medicine, The University of Tokyo
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- Inaba, Kenji
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University; Department of Molecular and Chemical Life Sciences, Graduate School of Life Sciences, Tohoku University; epartment of Chemistry, Graduate School of Science, Tohoku University; Medical Institute of Bioregulation, Kyushu University; Core Research for Evolutional Science and Technology (CREST), Japan Agency for Medical Research and Development (AMED)
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Description
Zinc ions (Zn²⁺) are vital to most cells, with the intracellular concentrations of Zn²⁺ being tightly regulated by multiple zinc transporters located at the plasma and organelle membranes. We herein present the 2.2-3.1 Å-resolution cryo-EM structures of a Golgi-localized human Zn²⁺/H+ antiporter ZnT7 (hZnT7) in Zn²⁺-bound and unbound forms. Cryo-EM analyses show that hZnT7 exists as a dimer via tight interactions in both the cytosolic and transmembrane (TM) domains of two protomers, each of which contains a single Zn²⁺-binding site in its TM domain. hZnT7 undergoes a TM-helix rearrangement to create a negatively charged cytosolic cavity for Zn²⁺ entry in the inward-facing conformation and widens the luminal cavity for Zn²⁺ release in the outward-facing conformation. An exceptionally long cytosolic histidine-rich loop characteristic of hZnT7 binds two Zn²⁺ ions, seemingly facilitating Zn²⁺ recruitment to the TM metal transport pathway. These structures permit mechanisms of hZnT7-mediated Zn²⁺ uptake into the Golgi to be proposed.
Journal
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- Nature Communications
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Nature Communications 14 2023-08-08
Springer Nature
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Keywords
Details 詳細情報について
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- CRID
- 1050015897173955072
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- ISSN
- 20411723
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- HANDLE
- 2433/284848
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- OpenAIRE
