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Originally published In Press as doi:10.1074/jbc.M212351200 on January 2, 2003

J. Biol. Chem., Vol. 278, Issue 11, 9176-9184, March 14, 2003
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Interactions between Na,K-ATPase alpha -Subunit ATP-binding Domains*

Charles J. CostaDagger §, Craig GattoDagger , and Jack H. Kaplan||

From the  Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97201, the Dagger  Department of Biological Sciences, Illinois State University, Normal, Illinois 61790, and the § Department of Biological Sciences, Eastern Illinois University, Charleston, Illinois 61920

The reaction mechanism of the Na,K-ATPase is thought to involve a number of ligand-induced conformational changes. The specific amino acid residues responsible for binding many of the important ligands have been identified; however, details of the specific conformational changes produced by ligand binding are largely undescribed. The experiments described in this paper begin to identify interactions between domains of the Na,K-ATPase alpha -subunit that depend on the presence of particular ligands. The major cytoplasmic loop (between TM4 and TM5), which we have previously shown contains the ATP-binding domain, was overexpressed in bacteria either with a His6 tag or as a fusion protein with glutathione S-transferase. We have observed that these polypeptides associate in the presence of MgATP. Incubation with [gamma -32P]ATP under conditions that result in phosphorylation of the full-length Na,K-ATPase did not result in 32P incorporation into either the His6 tag or glutathione S-transferase fusion proteins. The MgATP-induced association was strongly inhibited by prior modification of the fusion proteins with fluorescein isothiocyanate or by simultaneous incubation with 10 µM eosin, indicating that the effect of MgATP is due to interactions within the nucleotide-binding domain. These data are consistent with Na,K-ATPase associating within cells via interactions in the nucleotide-binding domains. Although any functional significance of these associations for ion transport remains unresolved, they may play a role in cell function and in modulating interactions between the Na,K-ATPase and other proteins.

* This work was supported by National Institutes of Health (NIH) Grant GM61583 and American Heart Association Grant 0030161N (to C. G.) and NIH Grant GM39500 (to J. H. K.).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: Dept. of Biochemistry and Molecular Biology, L224, Oregon Health & Science University, 3181 S. W. Sam Jackson Park Rd., Portland, OR 97201-3098. Tel.: 503-494-1001; Fax: 503-494-1002; E-mail: kaplanj@ohsu.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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