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A more recent version of this article appeared on February 13, 2004 Originally published In Press as doi:10.1074/jbc.M311218200 on December 18, 2003 Originally published In Press as doi:10.1074/jbc.M311218200 on December 9, 2003 Originally published In Press as doi:10.1074/jbc.M311218200 on November 27, 2003
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Papers In Press, published online ahead of print December 12, 2003
J. Biol. Chem, 10.1074/jbc.M311218200
Submitted on October 13, 2003
Revised on November 12, 2003
Accepted on November 27, 2003

Molecular mechanisms of Cl transport by the renal Na-K-Cl cotransporter: identification of an intracellular locus that may form part of a high affinity Cl-binding site

Edith Gagon, Marc J. Bergeron, Genevieve M. Brunet, Nikolas D. Daigle, Charles F. Simard, and Paul Isenring

Medicine, Laval University, Quebec, QC G1R2J6

Corresponding Author: paul.isenring{at}crhdq.ulaval.ca

The 2nd transmembrane domain (tm) of the secretory Na-K-Cl cotransporter (NKCC1)and of the kidney-specific isoform (NKCC2) has been shown to play an important role in cation transport. For NKCC2, by way of illustration, alternative splicing of exon 4, a 96-bp sequence from which tm2 is derived, leads to the formation of the NKCC2A and F variants that both exhibit unique affinities for cations. Interestingly, the NKCC2 variants also exhibit substantial differences in Cl affinity as well as in the residue composition of the first intracellular connecting segment (cs1a), which immediately follows tm2 and which too is derived from exon 4. In this study, we have prepared chimeras of the shark NKCC2A and F (saA and saF) to determine whether cs1a could play a role in Cl transport; here, tm2 or cs1a in saF was replaced by the corresponding domain from saA (generating saA/F or saF/A, respectively). Functional analyses of these chimeras have shown that cs1a-specific residues account for most of the A-F difference in Cl affinity. For example, Km(Cl)s were ~8 mM for saF/A and saA, and ~70 mM for saA/F and saF. Intriguingly, variant residues in


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