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Originally published In Press as doi:10.1074/jbc.M201009200 on April 19, 2002

J. Biol. Chem., Vol. 277, Issue 23, 20270-20276, June 7, 2002
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Distinct Regulatory Effects of the Na,K-ATPase gamma  Subunit*

Helen X. Pu, Rosemarie Scanzano, and Rhoda BlosteinDagger

From the Departments of Medicine and Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada

The two variants of the gamma  subunit of the rat renal sodium pump, gamma a and gamma b, have similar effects on the Na,K-ATPase. Both increase the affinity for ATP due to a shift in the enzyme's E1 left-right-arrow E2 conformational equilibrium toward E1. In addition, both increase K+ antagonism of cytoplasmic Na+ activation. To gain insight into the structural basis for these distinct effects, extramembranous N-terminal and C-terminal mutants of gamma  were expressed in rat alpha 1-transfected HeLa cells. At the N terminus, the variant-distinct region was deleted (gamma NDelta 7) or replaced by alanine residues (gamma N7A). At the C terminus, four (gamma aCDelta 4) or ten (gamma aCDelta 10) residues were deleted. None of these mutations abrogates the K+/Na+ antagonism as evidenced in a similar increase in K'Na seen at high (100 mM) K+ concentration. In contrast, the C-terminal as well as N-terminal deletions (gamma NDelta 7, gamma aCDelta 4, and gamma aCDelta 10) abolished the decrease in K'ATP seen with wild-type gamma a or gamma b. It is concluded that different regions of the gamma  chain mediate the distinct functional effects of gamma , and the effects can be long-range. In the transmembrane region, the impact of G41R replacement was analyzed since this mutation is associated with autosomal dominant renal Mg2+-wasting in man (Meij, I. C., Koenderink, J. B., van Bokhoven, H., Assink, K. F. H., Groenestege, W. T., de Pont, J. J. H. H. M., Bindels, R. J. M., Monnens, L. A. H., Van den Heuvel, L. P. W. J., and Knoers, N. V. A. M. (2000) Nat. Genet. 26, 265-266). The results show that Gly-41 right-arrow Arg prevents trafficking of gamma  but not alpha beta pumps to the cell surface and abrogates functional effects of gamma  on alpha beta pumps. These findings underscore a potentially important role of gamma  in affecting solute transport, in this instance Mg2+ reabsorption, consequent to its primary effect on the sodium pump.


* This work was supported by operating grants from the Canadian Institutes of Health Research (MT-3876) and the Kidney Foundation of Canada.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Montreal General Hospital, 1650 Cedar Ave., Montreal, Quebec H3G 1A4, Canada. Tel.: 514-934-1934 (ext. 44501); Fax: 514-934-8332; E-mail: Rhoda. Blostein{at}mcgill.ca.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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