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Fig. 2. Deglycosylation by site-directed mutagenesis also caused apical targeting of Na+/K+-ATPase ß-subunit. (A) Hep G2 cells transfected with control vector (Mock), the wild type (WT) or one of the three deglycosylated and FLAG-tagged ß-subunit genes (N124Q, N240Q, N124/240Q) were treated with tunicamycin (TM) or not (-) before western blot analyses using anti-FLAG antibody. The fully glycosylated (***ß), intermediately glycosylated (**ß), and the core (*ß) proteins of the Na+/K+-ATPase ß-subunit are indicated. (B) Hep G2 cells transfected with control vector (CTL), the wild-type (WT), or one of the three deglycosylated and FLAG-tagged ß-subunit genes (N124Q, N240Q, N124/240Q) were subjected to IF staining using anti-FLAG antibody (green in the merged panel); F-actin staining (red) was used to localize the apical domain (arrow). Note that the wild-type ß-subunit proteins were found only along the basolateral membrane (arrowheads), whereas all three mutants exhibited apical presence (double arrowheads). Bar, 5 µm.





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