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Originally published In Press as doi:10.1074/jbc.R100023200 on June 12, 2001

J. Biol. Chem., Vol. 276, Issue 32, 29617-29620, August 10, 2001
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MINIREVIEW
Ion Pumps in Polarized Cells: Sorting and Regulation of the Na+,K+- and H+,K+-ATPases*

Lisa A. Dunbar and Michael J. CaplanDagger

From the Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510

The physiologic function of an ion transport protein is determined, in part, by its subcellular localization and by the cellular mechanisms that modulate its activity. The Na+,K+-ATPase and the H+,K+-ATPases are closely related members of the P-type family of ion transporting ATPases. Despite their homology, these pumps are sorted to different domains in polarized epithelial cells, and their enzymatic activities are subject to distinct regulatory pathways. The molecular signals responsible for these properties have begun to be elucidated. It appears that a complex array of inter- and intramolecular interactions govern trafficking, distribution, and catalytic capacities of these proteins.

* This minireview will be reprinted in the 2001 Minireview Compendium, which will be available in December, 2001. This is the second article of two in the "Transport ATPase Trafficking Minireview Series." Work from the authors' laboratory presented here is supported by National Institutes of Health Grants GM-42136 and DK-17433.

Dagger To whom correspondence should be addressed: Dept. of Cellular and Molecular Physiology, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06510. Tel.: 203-785-7316; Fax: 203-785-4951; E-mail: michael.caplan@yale.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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