SLC30A1 Membrane Protein Introduction

Introduction of SLC30A1

Solute carrier family 30 member 1 (SLC30A1), also known as zinc transporter 1 (ZnT-1), is a protein which in humans is encoded by the SLC30A1 gene. As a member of the SLC30 (ZnT) family, it has the ability to modulate zinc permeation through the L-type calcium channel. In addition to downregulate Zn++ influx, it could also downregulate Ca++ influx, thereby protecting cells from the effects of excessive cation permeation.

Function of SLC30A1 Membrane Protein

SLC30A1 or ZNT1 belongs to the SLC30 family which was previously called the cation diffusion facilitator (CDF) family. With the simplest gene structure (only 2 exons), ZNT1 is characterized as six transmembrane domains with both N- and C-termini on the cytoplasmic side of the membrane. Studies have shown that it is the only member of this family that functions primarily as an exporter on the cell membrane to transport cytoplasmic zinc ions across the membrane to the extracellular space. It has been reported that SLC30A1 mRNA is expressed in trophoblasts and in the maternal decidua during the postimplantation period. What’s more, high dietary zinc intake could increase the expression of SLC30A1 in the intestine, brain, and placenta while low dietary zinc intake decreases SLC30A1 expression in these tissues.

Fig.1 Cooperative function of MT, ZnT1, and ZnT4 in the activation of zinc-requiring ectoenzymes. (Kimura, 2016)

Application SLC30A1 of Membrane Protein in Literature

1. Zogzas C.E. and Mukhopadhyay S. Putative metal binding site in the transmembrane domain of the manganese transporter SLC30A10 is different from that of related zinc transporters. Metallomics. 2018, 10(8):1053-1064. PubMed ID: 29989630
   
   

   This article aims to resolve the divergent results about the requirement of the crucial asparagine-43 residue. It suggests that the mechanisms of ion coordination within the transmembrane domain of SLC30A10 substantially differ from previously-studied CDFs, indicating that factors beyond site A residues may confer metal specificity to CDFs, and improve understanding of the pathobiology of manganese toxicity due to mutations in SLC30A10.

2. Pan R. and Liu K.J. ZNT-1 Expression Reduction Enhances Free Zinc Accumulation in Astrocytes After Ischemic Stroke. Acta Neurochir Suppl. 2016, 121:257-61. PubMed ID: 26463958
   
   

   This article investigates the effect of hypoxia/reoxygenation on ZnT-1 and ZIP-1. It suggests that hypoxia/reoxygenation blocks zinc efflux, whereas zinc influx may be at a similar level to that in normoxia, providing a novel mechanism for intracellular free zinc accumulation after ischemic stroke.

3. Liu C., et al. Suppression of placental metallothionein 1 and zinc transporter 1 mRNA expressions contributes to fetal heart malformations caused by maternal zinc deficiency. Cardiovascular toxicology. 2014, 14(4):329-38. PubMed ID: 24807795
   
   

   The article aims to investigate the association between placental MT-1 and ZnT-1 expressions with fetal heart malformations resulting from maternal zinc deficiency. Results suggest that maternal zinc deficiency results in an elevated incidence of fetal heart malformations, which is associated with significant decreases in placental MT-1 and ZnT-1 mRNA expressions to the levels below the threshold values that may be a crucial factor to determine the presence of fetal heart malformations.

4. Shusterman E., et al. ZnT-1 extrudes zinc from mammalian cells functioning as a Zn²⁺/H⁺ exchanger. Metallomics. 2014, 6(9):1656-63. PubMed ID: 24951051
   
   

   This article demonstrates that ZnT-1 extrudes zinc from mammalian cells by functioning as a Zn(2+)/H(+) exchanger.

5. Sindreu C., et al. Zinc transporter-1 concentrates at the postsynaptic density of hippocampal synapses. Molecular brain. 2014, 7(1):16. PubMed ID: 24602382
   
   

   This report suggests that ZnT1 is a novel postsynaptic density protein, and it may help elucidate the role of zinc homeostasis in synaptic function and disease.

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Reference

1. Kimura, et al. (2016). The functions of metallothionein and ZIP and ZnT transporters: an overview and perspective. International journal of molecular sciences. 17(3): 336.

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