The Na-K-ATPase α1β1 heterodimer as a cell adhesion molecule in epithelia

Olga Vagin*, Laura A. Dada, Elmira Tokhtaeva, George Sachs

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

52 Scopus citations

Abstract

The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. The review summarizes the data showing that, in addition to pumping ions, the Na-K-ATPase located at the sites of cell-cell junction acts as a cell adhesion molecule by interacting with the Na-K-ATPase of the adjacent cell in the intercellular space accompanied by anchoring to the cytoskeleton in the cytoplasm. The review also discusses the experimental evidence on the importance of a specific amino acid region in the extracellular domain of the Na-K-ATPase (β1 subunit for the Na-K-ATPase trans-dimerization and intercellular adhesion. Furthermore, a possible role of N-glycans linked to the Na-K-ATPase (β1 subunit in regulation of epithelial junctions by modulating β11 interactions is discussed.

Original languageEnglish (US)
Pages (from-to)C1271-C1281
JournalAmerican Journal of Physiology - Cell Physiology
Volume302
Issue number9
DOIs
StatePublished - May 1 2012

Keywords

  • Epithelial junctions
  • Na-k-atpase β subunit
  • Trans-dimerization

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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