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J Biol Chem, Vol. 274, Issue 47, 33183-33185, November 19, 1999

COMMUNICATION
The  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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