CD63 interacts with the carboxy terminus of the colonic H+-K+-ATPase to decrease [corrected] plasma membrane localization and 86Rb+ uptake.

ABSTRACT: 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 HKalpha(2), we selected 84 amino acids in the CT of the alpha-subunit of mouse colonic H(+)-K(+)-ATPase (CT-HKalpha(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-HKalpha(2) with CD63, recombinant CT-HKalpha(2) and CD63 were synthesized in vitro and incubated, and complexes were immunoprecipitated. CT-HKalpha(2) protein (but not CT-HKalpha(1)) coprecipitated with CD63, confirming stable assembly of HKalpha(2)

SUBMITTER: Codina J 

PROVIDER: S-EPMC1868892 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature