SLC50A1 Membrane Protein Introduction

Introduction of SLC50A1

SLC50A1 (solute carrier family 50, member 1), also known as sugar transporter SWEET1 or stromal cell protein (SCP), is a Na⁺-independent anion exchanger (AE). It belongs to the Slc4a family of Cl^-/HCO₃^- exchangers that contain products of 11 human genes (SLC4A1-5; A6, A7-11). They are composed of Na⁺-independent anion exchangers (AEs) SLC4A1 (AE1), SLC4A2 (AE2), SLC4A3 (AE3), and SLC50A1 (AE4) and Na⁺-coupled bicarbonate transporters (NBCs). There are structural and functional similarities between all transporters of the SLC4 gene family. AE polypeptides consist of three distinct domains: a hydrophilic cytoplasmic N-terminal domain of ~400-700 amino acids, a hydrophobic transmembrane domain of ~500 amino acids, and a cytoplasmic C-terminal consisting of ~30-100 amino acids.

Function of SLC50A1 Membrane Protein

SLC50A1 (AE4) is a membrane protein involved in anion exchange. It has been found to be expressed on the apical membrane of gastric mucous cells and duodenal epithelial cells in mouse, rabbit, and human. However, the function of AE4 in HCO₃^- secretion and chloride absorption in gastric and duodenal epithelial cells is not clear. Early research found that AE4 is a Na⁺-independent anion exchanger. However, a recent study revealed that it is an electroneutral monovalent cation-dependent Cl^-/HCO₃^- exchanger that mediates Cl^-/HCO₃^- exchange activity in the presence of K⁺ as well as Cs⁺, Li⁺, and Rb⁺. SLC4 family members have been shown to play an important role in exocrine gland fluid secretion by promoting intracellular Cl^- accumulation. Indeed. the expression of AE4 is found in secretory acinar cells such as salivary gland acinar cells and involved in the regulation of intracellular Cl^- accumulation in exchange for KHCO₃^- efflux. Mice lacking AE4 Cl^-/HCO₃^- exchangers will reduce HCO₃^--dependent Cl^- uptake and thus decrease saliva secretion. These suggest AE4 appears to play an important role in fluid secretion.

Fig.1 Na⁺-dependent HCO₃^-/HCO₃^- exchange under low Cl^- concentrations. (Peña-Münzenmayer, 2016)

Application of SLC50A1 Membrane Protein in Literature

1. Peña-Münzenmayer G., et al. Ae4 (SLC50A1) is an electroneutral monovalent cation-dependent Cl^-/HCO₃^- exchanger. Journal of General Physiology. 2016, 147(5): 423-436. PubMed ID: 27114614
   
   

   The study identifies SLC50A1 as an electroneutral Cl(-)/nonselective cation-HCO3(-) exchanger and demonstrates AE4 promotes Cl(-) influx in exchange for K(+)(Na(+)) and HCO3(-) ions in secretory cells.

2. Peñamünzenmayer G., et al. Ae4 (SLC50A1) Anion Exchangers Drive Cl- Uptake-dependent Fluid Secretion by Mouse Submandibular Gland Acinar Cells. Journal of Biological Chemistry. 2015, 290(17): 10677-10688. PubMed ID: 25745107
   
   

   The research makes a conclusion that AE4 is functionally expressed in submandibular acinar cells and involved in the cAMP-dependent regulation of fluid secretion.

3. Vera-Sigüenza E., et al. A Mathematical Model Supports a Key Role for Ae4 (SLC50A1) in Salivary Gland Secretion. Bulletin of Mathematical Biology. 2018, 80(2): 255-282. PubMed ID: 29209914
   
   

   In this study, a mathematical model of a salivary gland acinar cell is used to investigate the role of Ae2 (Slc4a2) and Ae4 (SLC50A1) in saliva secretion and the results show that Ae4 plays an important role in saliva secretion.

4. Purkerson J.M., et al. Insights into acidosis-induced regulation of SLC26A4 (pendrin) and SLC50A1 (AE4) transporters using three-dimensional morphometric analysis of β-intercalated cells. Am J Physiol Renal Physiol. 2014, 307(5): F601-11. PubMed ID: 24990900
   
   

   The aim of this study is to investigate the three-dimensional (3-D) expression and distribution of SLC26A4 and AE4 in β-intercalated cells (β-ICs) of the rabbit cortical collecting duct. And the results show that acidosis reduces AE4 expression in β-ICs and diminishes pendrin in apical recycling endosomes.

5. Kurth I., et al. The forkhead transcription factor Foxi1 directly activates the AE4 promoter. Biochemical Journal. 2006, 393(1): 277-83. PubMed ID: 16159312
   
   

   The article demonstrates that AE4 promoter appears to be a direct target of forkhead transcription factor Foxi1.

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Reference

1. Peña-Münzenmayer G, et al. (2016). Ae4 (SLC50A1) is an electroneutral monovalent cation-dependent Cl-/HCO3- exchanger. Journal of General Physiology. 147(5): 423-436.

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