ArticleJournal of cell science2012
Identification of the amino acid region involved in the intercellular interaction between the β1 subunits of Na+/K+ -ATPase.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Glycolytic activation of β-cell NaMolecular metabolism · 2026Article
- Connecting the Dots: AMOG/βInternational journal of molecular sciences · 2025Review
- Article
- In silico studies provide new structural insights into trans-dimerization of β1 and β2 subunits of the Na+, K+-ATPase.PloS one · 2025Article
- Recent Advances in the Study of NaCells · 2022Review
- The βInternational journal of molecular sciences · 2022Article
- Maturation of the Na,K-ATPase in the Endoplasmic Reticulum in Health and Disease.The Journal of membrane biology · 2021Article
- Article
- Article
- Identification of putative biomarkers for Infantile Hemangiomas and Propranolol treatment via data integration.Scientific reports · 2020Article
- Ouabain Accelerates Collective Cell Migration Through a cSrc and ERK1/2 Sensitive Metalloproteinase Activity.The Journal of membrane biology · 2019Article
- A Functional Interaction Between Na,K-ATPase βMolecular neurobiology · 2019Article
- A Model for the Homotypic Interaction between NaInternational journal of molecular sciences · 2019Article
- Regulation of Neuronal Na,K-ATPase by Extracellular Scaffolding Proteins.International journal of molecular sciences · 2018Article
- The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell-cell trans-dimerization of Na,K-ATPase β1 subunits.Journal of cell science · 2016Article
- β1-Na(+),K(+)-ATPase gene therapy upregulates tight junctions to rescue lipopolysaccharide-induced acute lung injury.Gene therapy · 2016Article
- Septin dynamics are essential for exocytosis.The Journal of biological chemistry · 2015Article
- Recruitment of septin cytoskeletal proteins by botulinum toxin A protease determines its remarkable stability.Journal of cell science · 2014Article
- The kinase domains of obscurin interact with intercellular adhesion proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Na(+),K (+)-ATPase as a docking station: protein-protein complexes of the Na(+),K (+)-ATPase.Cellular and molecular life sciences : CMLS · 2013Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Epithelial junctions depend on intercellular interactions between β(1) subunits of the Na(+)/K(+)-ATPase molecules of neighboring cells. The interaction between dog and rat subunits is less effective than the interaction between two dog β(1) subunits, indicating the importance of species-specific regions for β(1)-β(1) binding. To identify these regions, the species-specific amino acid residues were mapped on a high-resolution structure of the Na(+)/K(+)-ATPase β(1) subunit to select those exposed towards the β(1) subunit of the neighboring cell. These exposed residues were mutated in both dog and rat YFP-linked β(1) subunits (YFP-β(1)) and also in the secreted extracellular domain of the dog β(1) subunit. Five rat-like mutations in the amino acid region spanning residues 198-207 of the dog YFP-β(1) expressed in Madin-Darby canine kidney (MDCK) cells decreased co-precipitation of the endogenous dog β(1) subunit with YFP-β(1) to the level observed between dog β(1) and rat YFP-β(1). In parallel, these mutations impaired the recognition of YFP-β(1) by the dog-specific antibody that inhibits cell adhesion between MDCK cells. Accordingly, dog-like mutations in rat YFP-β(1) increased both the (YFP-β(1))-β(1) interaction in MDCK cells and recognition by the antibody. Conversely, rat-like mutations in the secreted extracellular domain of the dog β(1) subunit increased its interaction with rat YFP-β(1) in vitro. In addition, these mutations resulted in a reduction of intercellular adhesion between rat lung epithelial cells following addition of the secreted extracellular domain of the dog β(1) subunit to a cell suspension. Therefore, the amino acid region 198-207 is crucial for both trans-dimerization of the Na(+)/K(+)-ATPase β(1) subunits and cell-cell adhesion.
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