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Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus
Open accessPreprint — published as 10.1038/s41467-023-40521-5
Abstract
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 2.8-2.9 Å-resolution cryo-EM structures of a Golgi-localized human Zn2+/H+ antiporter ZnT7 (hZnT7) in its outward- and inward-facing forms. Cryo-EM analyses showed that hZnT7 exists as a homodimer via tight interactions in both the cytosolic and transmembrane (TM) regions 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 form and a widened luminal cavity for Zn2+ release in the outward-facing form. An exceptionally long cytosolic histidine-rich loop characteristic of hZnT7 can bind at least two Zn2+ ions, likely facilitating Zn2+ recruitment from the cytosol. Unique mechanisms of hZnT7-mediated Zn2+ uptake into the Golgi are proposed.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Bui, H., Watanabe, S., Nomura, N., Liu, K., Uemura, T., Inoue, M., Tsutsumi, A., Fujita, H., Kinoshita, K., Iwata, S., Kikkawa, M., & Inaba, K.
- Affiliations
- Tohoku University (JP)
- Kyoto University (JP)
- The University of Tokyo (JP)
- Canon Medical Systems Corporation (Japan) (JP)
- Kyushu University (JP)
- Corresponding author
- Inaba, Kenji
- ORCID
- Venue
- Nature Communications
- Published
- 2022-09-23
- Volume
- 14
- Issue
- 1
- Pages
- 4770-4770
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10409766
- OpenAlex
- W4385666618
- Cited by
- 34
- References
- 1
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 10 · 2023: 6
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Kyoto University Research Information Repository (Kyoto University) (submittedVersion, cc-by)
- Funders
- Japan Agency for Medical Research and Development (JP19am0101115, CREST, JP22ama121038, JP19am0101078, JP21am0101079, 21gm1410006h0001, 21H04758, 18H03978, 21H05247)
- Canon Medical Systems Corporation
- Ministry of Education, Culture, Sports, Science and Technology (18H03978, 21H04758, 21H05247)
- Japan Society for the Promotion of Science (21gm1410006h0001, 21H05248, 21H05247, JP21am0101079, 23K27415, 21H04758, JP22ama121038, JP19am0101115, CREST, 19H00923, 19H05777, 18H03978, 23K18239)
- Core Research for Evolutional Science and Technology (21gm1410006h0001)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- zinc transporters, Golgi apparatus, zinc uptake, protein dimerization, zinc binding site, inward-facing conformation, zinc homeostasis, membrane protein structure
- MeSH terms
- Carrier Proteins, Golgi Apparatus, Humans, Zinc, Cryoelectron Microscopy, Cation Transport Proteins
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