Abstract
The SLC26 family of anion transporters consists of 10 members that display remarkable functional and substrate diversity. Mutations in several members of the family have been identified as causing a variety of human diseases and mouse phenotype when deleted. The family drew the attention and strong interest of epithelial biologist with the identification of the first elusive luminal Cl−/HCO3− exchange, which turned to be the third member of the family SLC26A3. Fairly quick, progress since revealed that members of the family transport all halides, NO3−, SO42−, oxalate, and formate, among others. Members of the family can be grouped into three subgroups based on substrate selectivity and transport mode: the SO42− transporters SLC26A1 and SLC26A2; the anion exchangers 2Cl−/1HCO3− SLC26A3, 1Cl−/1HCO3− SLC26A4, and 1Cl−/2HCO3− SLC26A6; and the Cl− channels SLC26A7, SLC26A9, and SLC26A11. This chapter discusses structural features, transport properties, and regulation of the transporters that are essential to understand their functions and roles in human diseases.
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