The Polarized Distribution of Na+,K+-ATPase: Role of the Interaction between β Subunits
Open Access
- 1 July 2010
- journal article
- Published by American Society for Cell Biology (ASCB) in Molecular Biology of the Cell
- Vol. 21 (13) , 2217-2225
Abstract
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 β 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 β subunits have sufficient proximity and affinity to permit a direct interaction, without requiring any additional extracellular molecules to span the distance.Keywords
This publication has 68 references indexed in Scilit:
- Apical trafficking in epithelial cells: signals, clusters and motorsJournal of Cell Science, 2009
- Assembly with the Na,K-ATPase α1 Subunit Is Required for Export of β1 and β2 Subunits from the Endoplasmic ReticulumBiochemistry, 2009
- Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cellsJournal of Cell Biology, 2009
- Coordinated protein sorting, targeting and distribution in polarized cellsNature Reviews Molecular Cell Biology, 2008
- AP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cellsProceedings of the National Academy of Sciences, 2007
- On the self-association potential of transmembrane tight junction proteinsCellular and Molecular Life Sciences, 2006
- Organization of vesicular trafficking in epitheliaNature Reviews Molecular Cell Biology, 2005
- Role of the second immunoglobulin-like loop of nectin in cell–cell adhesionBiochemical and Biophysical Research Communications, 2002
- Mutation of the Protein Kinase C Phosphorylation Site on Rat α1 Na+,K+-ATPase Alters Regulation of Intracellular Na+ and pH and Influences Cell Shape and AdhesivenessJournal of Biological Chemistry, 1997
- Occluding junctions in a cultured transporting epithelium: Structural and functional heterogeneityThe Journal of Membrane Biology, 1980