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Am J Physiol Cell Physiol 288: C1279-C1286, 2005. First published January 12, 2005; doi:10.1152/ajpcell.00463.2004
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MEMBRANE TRANSPORTERS, ION CHANNELS, AND PUMPS

CD63 interacts with the carboxy terminus of the colonic H+-K+-ATPase to increase plasma membrane localization and 86Rb+ uptake

Juan Codina, Jian Li, and Thomas D. DuBose, Jr.

Sections on Nephrology and Molecular Medicine, Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, North Carolina

Submitted 20 September 2004 ; accepted in final form 10 January 2005

The carboxy terminus (CT) of the colonic H+-K+-ATPase is required for stable assembly with the {beta}-subunit, translocation to the plasma membrane, and efficient function of the transporter. To identify protein-protein interactions involved in the localization and function of HK{alpha}2, we selected 84 amino acids in the CT of the {alpha}-subunit of mouse colonic H+-K+-ATPase (CT-HK{alpha}2) as the bait in a yeast two-hybrid screen of a mouse kidney cDNA library. The longest identified clone was CD63. To characterize the interaction of CT-HK{alpha}2 with CD63, recombinant CT-HK{alpha}2 and CD63 were synthesized in vitro and incubated, and complexes were immunoprecipitated. CT-HK{alpha}2 protein (but not CT-HK{alpha}1) coprecipitated with CD63, confirming stable assembly of HK{alpha}2 with CD63. In HEK-293 transfected with HK{alpha}2 plus {beta}1-Na+-K+-ATPase, suppression of CD63 by RNA interference increased cell surface expression of HK{alpha}2/NK{beta}1 and 86Rb+ uptake. These studies demonstrate that CD63 participates in the regulation of the abundance of the HK{alpha}2-NK{beta}1 complex in the cell membrane.

protein assembly; cell surface localization


Address for reprint requests and other correspondence: T. D. DuBose, Jr., Dept. of Internal Medicine, Wake Forest Univ. School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157 (E-mail: tdubose{at}wfubmc.edu)




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