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Human NKCC2 cation–Cl – co‐transporter complements lack of Vhc1 transporter in yeast vacuolar membranes
Author(s) -
Petrezselyova Silvia,
Dominguez Angel,
Herynkova Pavla,
Macias Juan F.,
Sychrova Hana
Publication year - 2013
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.2976
Subject(s) - transporter , saccharomyces cerevisiae , yeast , alkali metal , membrane , chloride , biochemistry , mutant , salt (chemistry) , organic cation transport proteins , biology , membrane transport protein , chemistry , biophysics , gene , organic chemistry
Cation–chloride co‐transporters serve to transport Cl – and alkali metal cations. Whereas a large family of these exists in higher eukaryotes, yeasts only possess one cation–chloride co‐transporter, Vhc1, localized to the vacuolar membrane. In this study, the human cation–chloride co‐transporter NKCC2 complemented the phenotype of VHC1 deletion in Saccharomyces cerevisiae and its activity controlled the growth of salt‐sensitive yeast cells in the presence of high KCl, NaCl and LiCl. A S . cerevisiae mutant lacking plasma‐membrane alkali–metal cation exporters Nha1 and Ena1‐5 and the vacuolar cation–chloride co‐transporter Vhc1 is highly sensitive to increased concentrations of alkali–metal cations, and it proved to be a suitable model for characterizing the substrate specificity and transport activity of human wild‐type and mutated cation–chloride co‐transporters. Copyright © 2013 John Wiley & Sons, Ltd.