Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells
Zinc is an important trace metal in immune systems, and zinc transporters are involved in many immune responses. Recent advances have revealed the structural and biochemical bases for zinc transport across the cell membrane, with clinical implications for the regulation of zinc homeostasis in immune...
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| Format: | Article |
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Wiley
2018-01-01
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| Series: | Journal of Immunology Research |
| Online Access: | http://dx.doi.org/10.1155/2018/9365747 |
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| author | Bum-Ho Bin Juyeon Seo Sung Tae Kim |
| author_facet | Bum-Ho Bin Juyeon Seo Sung Tae Kim |
| author_sort | Bum-Ho Bin |
| collection | DOAJ |
| description | Zinc is an important trace metal in immune systems, and zinc transporters are involved in many immune responses. Recent advances have revealed the structural and biochemical bases for zinc transport across the cell membrane, with clinical implications for the regulation of zinc homeostasis in immune cells like dendritic cells, T cells, B cells, and mast cells. In this review, we discuss the function, structure, and transport aspects of two major mammalian zinc transporter types, importers and exporters. First, Zrt-/Irt-like proteins (ZIPs) mediate the zinc influx from the extracellular or luminal side into the cytoplasm. There are 14 ZIP family members in humans. They form a homo- or heterodimer with 8 transmembrane domains and extra-/intracellular domains of various lengths. Several ZIP members show specific extracellular domains composed of two subdomains, a helix-rich domain and proline-alanine-leucine (PAL) motif-containing domain. Second, ZnT (zinc transporter) was initially identified in early studies of zinc biology; it mediates zinc efflux as a counterpart of ZIPs in zinc homeostasis. Ten family members have been identified. They show a unique architecture characterized by a Y-shaped conformation and a large cytoplasmic domain. A precise, comprehensive understanding of the structures and transport mechanisms of ZIP and ZnT in combination with mice experiments would provide promising drug targets as well as a basis for identifying other transporters with therapeutic potential. |
| format | Article |
| id | doaj-art-027c08b14cbe4f79a845e0ae84a7ad34 |
| institution | Kabale University |
| issn | 2314-8861 2314-7156 |
| language | English |
| publishDate | 2018-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Immunology Research |
| spelling | doaj-art-027c08b14cbe4f79a845e0ae84a7ad342025-02-03T05:45:24ZengWileyJournal of Immunology Research2314-88612314-71562018-01-01201810.1155/2018/93657479365747Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune CellsBum-Ho Bin0Juyeon Seo1Sung Tae Kim2Department of Molecular Science and Technology, College of Natural Sciences, Ajou University, Suwon 16499, Republic of KoreaBasic Research & Innovation Division, AmorePacific R&D Unit, Yongin 17014, Republic of KoreaDepartment of Pharmaceutical Engineering, Inje University, Gimhae 50834, Republic of KoreaZinc is an important trace metal in immune systems, and zinc transporters are involved in many immune responses. Recent advances have revealed the structural and biochemical bases for zinc transport across the cell membrane, with clinical implications for the regulation of zinc homeostasis in immune cells like dendritic cells, T cells, B cells, and mast cells. In this review, we discuss the function, structure, and transport aspects of two major mammalian zinc transporter types, importers and exporters. First, Zrt-/Irt-like proteins (ZIPs) mediate the zinc influx from the extracellular or luminal side into the cytoplasm. There are 14 ZIP family members in humans. They form a homo- or heterodimer with 8 transmembrane domains and extra-/intracellular domains of various lengths. Several ZIP members show specific extracellular domains composed of two subdomains, a helix-rich domain and proline-alanine-leucine (PAL) motif-containing domain. Second, ZnT (zinc transporter) was initially identified in early studies of zinc biology; it mediates zinc efflux as a counterpart of ZIPs in zinc homeostasis. Ten family members have been identified. They show a unique architecture characterized by a Y-shaped conformation and a large cytoplasmic domain. A precise, comprehensive understanding of the structures and transport mechanisms of ZIP and ZnT in combination with mice experiments would provide promising drug targets as well as a basis for identifying other transporters with therapeutic potential.http://dx.doi.org/10.1155/2018/9365747 |
| spellingShingle | Bum-Ho Bin Juyeon Seo Sung Tae Kim Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells Journal of Immunology Research |
| title | Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells |
| title_full | Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells |
| title_fullStr | Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells |
| title_full_unstemmed | Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells |
| title_short | Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells |
| title_sort | function structure and transport aspects of zip and znt zinc transporters in immune cells |
| url | http://dx.doi.org/10.1155/2018/9365747 |
| work_keys_str_mv | AT bumhobin functionstructureandtransportaspectsofzipandzntzinctransportersinimmunecells AT juyeonseo functionstructureandtransportaspectsofzipandzntzinctransportersinimmunecells AT sungtaekim functionstructureandtransportaspectsofzipandzntzinctransportersinimmunecells |