Unusual degradation of α-β complexes inXenopusoocytes by β-subunits ofXenopusgastric H-K-ATPase
The catalytic α-subunit of oligomeric P-type ATPases such as Na-K-ATPase and H-K-ATPase requires association with a β-subunit after synthesis in the endoplasmic reticulum (ER) to become stably expressed and functionally active. In this study, we have expressed the β-subunit of Xenopus gastric H-K-ATPase (βHK) in Xenopus oocytes together with α-subunits of H-K-ATPase (αHK) or Na-K-ATPase (αNK) and have followed the biosynthesis, assembly, and cell surface expression of functional pumps. Immunoprecipitations of Xenopus βHK from metabolically labeled oocytes show that it is well expressed and, when synthesized without α-subunits, can leave the ER and become fully glycosylated. Xenopus βHK can associate with both coexpressed αHK and αNK, but the α-β complexes formed are degraded rapidly in or close to the ER and do not produce functional pumps at the cell surface as assessed by86Rb uptake. A possible explanation of these results is that Xenopus βHK may contain a tissue-specific signal that is important in the formation or correct targeting of functional α-β complexes in the stomach but that cannot be recognized in Xenopusoocytes and in consequence leads to cellular degradation of the α-β complexes in this experimental system.