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Am J Physiol Cell Physiol (January 12, 2005). doi:10.1152/ajpcell.00463.2004
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Submitted on September 20, 2004
Accepted on January 10, 2005

CD63 Interacts with the Carboxy-Terminus of the Colonic H+,K+-ATPase to Increase Plasma Membrane Localization and Rb+-Uptake

Juan Codina1, Jian Li1, and Thomas D. DuBose, Jr.1*

1 Internal Medicine/Nephrology, Wake Forest University School of Medicine, Winston-Salem, NC, USA

* To whom correspondence should be addressed. E-mail: tdubose{at}wfubmc.edu.

The carboxy-terminus 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 carboxy-terminus 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 interaction of CT-HK{alpha}2 with CD63, recombinant CT-HK{alpha}2 and CD63 were synthesized in vitro, incubated, and complexes immunoprecipitated. CT-HK{alpha}2 protein (but not CT-HK{alpha}1) co-precipitated 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.




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