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Am J Physiol Cell Physiol 284: C769-C779, 2003. First published November 20, 2002; doi:10.1152/ajpcell.00270.2002
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Vol. 284, Issue 3, C769-C779, March 2003

Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains

Hannes Lohi1, Georg Lamprecht2, Daniel Markovich3, Anders Heil2, Minna Kujala1, Ursula Seidler2, and Juha Kere1,4,5

1 Department of Medical Genetics, Biomedicum Helsinki, and 4 Finnish Genome Center, University of Helsinki, 00014 Helsinki, Finland; 2 Department I of Medicine, Eberhard-Karls University, Tübingen, Germany; 3 Department of Physiology and Pharmacology, School of Biomedical Sciences, University of Queensland, Brisbane, Queensland 4072, Australia; and 5 Department of Biosciences, Novum, Karolinska Institute, 14157 Huddinge, Sweden

The solute carrier gene family SLC26 consists of tissue-specific anion exchanger genes, three of them associated with distinct human recessive disorders. By a genome-driven approach, several new SLC26 family members have been identified, including a kidney- and pancreas-specific gene, SLC26A6. We report the functional characterization of SLC26A6 and two new alternatively spliced variants, named SLC26A6c and SLC26A6d. Immunofluorescence studies on transiently transfected cells indicated membrane localization and indicated that both NH2- and COOH-terminal tails of the SLC26A6 variants are located intracellularly, suggesting a topology with an even number of transmembrane domains. Functional expression of the three proteins in Xenopus oocytes demonstrated Cl- and SO<UP><SUB>4</SUB><SUP>2−</SUP></UP> transport activity. In addition, the transport of SO<UP><SUB>4</SUB><SUP>2−</SUP></UP> and Cl- was inhibited by DIDS and HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>. We demonstrated also that the COOH terminus of SLC26A6 binds to the first and second PDZ domains of the Na+/H+ exchanger (NHE)3 kinase A regulatory protein (E3KARP) and NHE3 regulatory factor (NHERF) proteins in vitro. Truncation of the last three amino acids (TRL) of SLC26A6 abrogated the interaction but did not affect transport function. These results demonstrate that SLC26A6 and its two splice variants can function as anion transporters linked to PDZ-interaction pathways. Our results support the general concept of microdomain organization for ion transport and suggest a mechanism for cystic fibrosis transmembrane regulator (CFTR)-mediated SLC26A6 upregulation in pancreatic duct cells.

alternative splicing; PDZ domain; SLC26


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