title: Characterization of the L683P mutation of SLC26A9 in Xenopus oocytes.
abstract: In the present study, we characterized a STAS-domain amino acid mutation of SLC26A9 having a significant impact on ion transport. We focused on the sole conserved L- leucine residue of the STAS domain identified among SLC26 members. We therefore characterized the L683P mutation of SLC26A9 in Xenopus oocytes by monitoring the protein functional expression (two-electrode technique for voltage-clamp analysis) and its presence at the cell membrane (surface protein biotinylation technique). This mutation was found to reduce Cl(-) transport through SLC26A9 as well as the positive interaction exerted by SLC26A9 on CFTR ion transport activity. The origin of this effect is discussed in the light of the presence of the SLC26A9-L683P mutant at the plasma membrane.
authors: Universite de Nice, Nice, Cedex 2, France.
authors: Martine
authors: M
authors: Avella
authors: Franck
authors: F
authors: Borgese
authors: Jordi
authors: J
authors: Ehrenfeld
mesh_terms: D000818:Animals; D000954:Antigens, Surface / Q000378:metabolism; D017920:Antiporters / Q000235:genetics* / Q000378:metabolism; D019921:Biotinylation; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000378:metabolism; D006801:Humans; D009154:Mutation / Q000235:genetics*; D009865:Oocytes / Q000378:metabolism; D000076988:Sulfate Transporters; D014982:Xenopus laevis
chemical_list: D000954:Antigens, Surface; D017920:Antiporters; C455628:SLC26A9 protein, human; D000076988:Sulfate Transporters; D019005:Cystic Fibrosis Transmembrane Conductance Regulator