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• W2081315017 abstract "The level of the heterodimeric Na,K-ATPase is tightly controlled in epithelia to maintain appropriate transport function. The catalytic Na,K-ATPase α subunit is not able to exit the ER or catalyze ion transport unless assembled with the β subunit. However, requirements for the ER exit of the Na,K-ATPase β subunit that plays an additional, ion-transport-independent, role in intercellular adhesion are not clear. Exogenous β1 or β2 subunits expressed in renal MDCK cells replace endogenous β1 subunits in the α−β complexes in the ER, resulting in a decrease in the amount of the α1-bound endogenous β1 subunits by 47−61% with no change in the amount of α1 subunits. Disruption of the α1−β association by mutations in defined α1-interacting regions of either β1 or β2 subunits results in the ER retention and rapid degradation of unassembled mutants. Hence, the ER quality control system allows export only of assembled α−β complexes to the Golgi, thereby maintaining an equimolar ratio of α and β subunits in the plasma membrane, whereas the number of α1 subunits in the ER determines the amount of the α−β complexes." @default.
• W2081315017 created "2016-06-24" @default.
• W2081315017 creator A5018386037 @default.
• W2081315017 creator A5019676161 @default.
• W2081315017 creator A5057185561 @default.
• W2081315017 date "2009-11-10" @default.
• W2081315017 modified "2023-09-24" @default.
• W2081315017 title "Assembly with the Na,K-ATPase α₁ Subunit Is Required for Export of β₁ and β₂ Subunits from the Endoplasmic Reticulum" @default.
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• W2081315017 doi "https://doi.org/10.1021/bi901438z" @default.
• W2081315017 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2987690" @default.
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• W2081315017 hasPublicationYear "2009" @default.
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