Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn²⁺ uptake into the Golgi apparatus
-
- 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
-
- 渡部, 聡
- 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
-
- 野村, 紀通
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
-
- 劉, 紅
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
-
- 植村, 智子
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
-
- 井上, 道雄
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
-
- 包, 明久
- Graduate School of Medicine, The University of Tokyo
-
- 藤田, 浩之
- Advanced Research Laboratory, Canon Medical Systems Corporation
-
- 木下, 賢吾
- Department of System Bioinformatics, Graduate School of Information Sciences, Tohoku University; Department of Integrative Genomics, Tohoku Medical Megabank Organization, Tohoku University
-
- 加藤, 幸成
- Graduate School of Medicine, Tohoku University
-
- 岩田, 想
- Department of Cell Biology, Graduate School of Medicine, Kyoto University
-
- 吉川, 雅英
- Graduate School of Medicine, The University of Tokyo
-
- 稲葉, 謙次
- 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)
書誌事項
- 公開日
- 2023-08-08
- 資源種別
- journal article
- 権利情報
-
- © The Author(s) 2023
- This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
- 公開者
- Springer Nature
この論文をさがす
説明
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.
収録刊行物
-
- Nature Communications
-
Nature Communications 14 2023-08-08
Springer Nature
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1050015897173955072
-
- ISSN
- 20411723
-
- HANDLE
- 2433/284848
-
- 本文言語コード
- en
-
- 資料種別
- journal article
-
- データソース種別
-
- IRDB
- OpenAIRE
