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J. Biol. Chem., Vol. 277, Issue 12, 10162-10172, March 22, 2002
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From the Laboratory of Membrane Biology, Neuroscience Center,
Massachusetts General Hospital, Charlestown, Massachusetts 02129
Sodium and potassium-exchanging adenosine
triphosphatase (Na,K-ATPase) in the kidney is associated with the
Differential Regulation of Renal Na,K-ATPase by Splice Variants
of the
Subunit*
subunit (, FXYD2), a single-span membrane protein that modulates
ATPase properties. Rat and human occur in two splice variants, a
and b, with different N termini. Here we investigated their
structural heterogeneity and functional effects on Na,K-ATPase
properties. Both forms were post-translationally modified during
in vitro translation with microsomes, indicating that there
are four possible forms of . Site-directed mutagenesis revealed
Thr2 and Ser5 as potential sites for
post-translational modification. Similar modification can occur in
cells, with consequences for Na,K-ATPase properties. We showed
previously that stable transfection of a into NRK-52E cells resulted
in reduction of apparent affinities for Na+ and
K+. Individual clones differed in post-translational modification, however, and the effect on
Na+ affinity was absent in clones with full modification.
Here, transfection of b also resulted in clones with or without
post-translational modification. Both groups showed a reduction
in Na+ affinity, but modification was required for the
effect on K+ affinity. There were minor increases in ATP
affinity. The physiological importance of the reduction in
Na+ affinity was shown by the slower growth of a, b,
and b' transfectants in culture. The differential influence of the
four structural variants of on affinities of the Na,K-ATPase for
Na+ and K+, together with our previous finding
of different distributions of a and b along the rat nephron,
suggests a highly specific mode of regulation of sodium pump properties
in kidney.
*
This work was supported by National Institutes of Health
Grant HL27653 (to K. J. S.).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.
To whom correspondence should be addressed: 149-6118, Massachusetts General Hospital, 149 13th St., Charlestown, MA 02129. Tel.: 617-726-8579; Fax: 617-726-7526; E-mail:
sweadner@helix.mgh.harvard.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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