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J Biol Chem, Vol. 274, Issue 47, 33183-33185, November 19, 1999
Subunit Modulates Na+ and K+
Affinity of the Renal Na,K-ATPase
From the Laboratory of Membrane Biology, Neuroscience Center,
Massachusetts General Hospital, Charlestown, Massachusetts 02129
The Na+,K+-ATPase
catalyzes the active transport of ions. It has two necessary subunits,
and
, but in kidney it is also associated with a 7.4-kDa
protein, the
subunit. Stable transfection was used to determine the
effect of
on Na,K-ATPase properties. When isolated from either
kidney or transfected cells, 

had lower affinities for both
Na+ and K+ than 
. A post-translational
modification of
selectively eliminated the effect on
Na+ affinity, suggesting three configurations (
,


, and 

*) conferring different stable properties to
Na,K-ATPase. In the nephron, segment-specific differences in
Na+ affinity have been reported that cannot be explained by
the known
and
subunit isoforms of Na,K-ATPase.
Immunofluorescence was used to detect
in rat renal cortex. Cortical
ascending limb and some cortical collecting tubules lacked
,
correlating with higher Na+ affinities in those segments
reported in the literature. Selective expression in different segments
of the nephron is consistent with a modulatory role for the
subunit
in renal physiology.
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