The polarized distribution of Na+,K+-ATPase: role of the interaction between {beta} subunits

The very existence of higher metazoans depends on the vectorial transport of substances across epithelia. A crucial element of this transport is the membrane enzyme Na(+),K(+)-ATPase. Not only is this enzyme distributed in a polarized manner in a restricted domain of the plasma membrane but also it...

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Bibliographic Details
Published in:Molecular biology of the cell 2010-07, Vol.21 (13), p.2217-2225
Main Authors: Padilla-Benavides, Teresita, Roldán, María L, Larre, Isabel, Flores-Benitez, David, Villegas-Sepúlveda, Nicolas, Contreras, Ruben G, Cereijido, Marcelino, Shoshani, Liora
Format: Article
Language:English
Subjects:
Animals
Cell Line
Cell Polarity
Cricetinae
Cricetulus
Dogs
Epithelial Cells - cytology
Epithelial Cells - metabolism
Fluorescence Resonance Energy Transfer
Models, Molecular
Protein Binding
Protein Conformation
Protein Isoforms - chemistry
Protein Isoforms - genetics
Protein Isoforms - metabolism
Protein Subunits - chemistry
Protein Subunits - genetics
Protein Subunits - metabolism
Rats
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Sodium-Potassium-Exchanging ATPase - chemistry
Sodium-Potassium-Exchanging ATPase - genetics
Sodium-Potassium-Exchanging ATPase - metabolism
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Summary:The very existence of higher metazoans depends on the vectorial transport of substances across epithelia. A crucial element of this transport is the membrane enzyme Na(+),K(+)-ATPase. Not only is this enzyme distributed in a polarized manner in a restricted domain of the plasma membrane but also it creates the ionic gradients that drive the net movement of glucose, amino acids, and ions across the entire epithelium. In a previous work, we have shown that Na(+),K(+)-ATPase polarity depends on interactions between the beta subunits of Na(+),K(+)-ATPases located on neighboring cells and that these interactions anchor the entire enzyme at the borders of the intercellular space. In the present study, we used fluorescence resonance energy transfer and coprecipitation methods to demonstrate that these beta subunits have sufficient proximity and affinity to permit a direct interaction, without requiring any additional extracellular molecules to span the distance.
ISSN:1939-4586
DOI:10.1091/mbc.E10-01-0081