ArticleMolecular biology of the cell1999
Insulin-induced stimulation of Na+,K(+)-ATPase activity in kidney proximal tubule cells depends on phosphorylation of the alpha-subunit at Tyr-10.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 103 citations in OpenAlex.
- Na/K-ATPase in the renal proximal tubule cell: classic & novel roles in sodium handling.Frontiers in physiology · 2026Review
- Glycolytic activation of β-cell NaMolecular metabolism · 2026Article
- Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications.Frontiers in cell and developmental biology · 2026Review
- Molecular Basis of Na, K-ATPase Regulation of Diseases: Hormone and FXYD2 Interactions.International journal of molecular sciences · 2024Review
- Insulin Resistance and Hypertension: Mechanisms Involved and Modifying Factors for Effective Glucose Control.Biomedicines · 2023Review
- Ang II acutely stimulates Na,K-pump in cells from proximal tubules by increasing its phosphorylation at S938 via a PI3K/AKT pathway.Physiological reports · 2022Article
- GNature communications · 2022Article
- Activation of Piezo1 Increases Na,K-ATPase-Mediated Ion Transport in Mouse Lens.International journal of molecular sciences · 2022Article
- Phosphorylation of NaThe Journal of membrane biology · 2021Article
- The role of AMPK in regulation of NaJournal of muscle research and cell motility · 2021Review
- Lyn regulates creatine uptake in an imatinib-resistant CML cell line.Biochimica et biophysica acta. General subjects · 2020Article
- Unique Regulation of Na-K-ATPase during Growth and Maturation of Intestinal Epithelial Cells.Cells · 2019Article
- Cyclic AMP-dependent protein kinase A and EPAC mediate VIP and secretin stimulation of PAK4 and activation of NaAmerican journal of physiology. Gastrointestinal and liver physiology · 2019Article
- Insulin receptors in the kidneys in health and disease.World journal of nephrology · 2019Review
- Na/K-ATPase Y260 Phosphorylation-mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth.Scientific reports · 2018Article
- Hyperglycaemia induced by chronic i.p. and oral glucose loading leads to hypertension through increased NaExperimental physiology · 2018Article
- Polyamines regulate phosphorylation-dephosphorylation kinetics in a crustacean gill (NaMolecular and cellular biochemistry · 2017Article
- Molecular characterization and expression of NaFish physiology and biochemistry · 2016Article
- Chronic insulin treatment phosphorylates the renal Na-K-ATPase α1-subunit at serine 16/23 and reduces its activity involving PI3-kinase-dependent PKC activation.American journal of physiology. Renal physiology · 2016Article
- Paediatrics, insulin resistance and the kidney.Pediatric nephrology (Berlin, Germany) · 2015Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Phosphorylation of the alpha-subunit of Na+,K(+)-ATPase plays an important role in the regulation of this pump. Recent studies suggest that insulin, known to increase solute and fluid reabsorption in mammalian proximal convoluted tubule (PCT), is stimulating Na+,K(+)-ATPase activity through the tyrosine phosphorylation process. This study was therefore undertaken to evaluate the role of tyrosine phosphorylation of the Na+,K(+)-ATPase alpha-subunit in the action of insulin. In rat PCT, insulin and orthovanadate (a tyrosine phosphatase inhibitor) increased tyrosine phosphorylation level of the alpha-subunit more than twofold. Their effects were not additive, suggesting a common mechanism of action. Insulin-induced tyrosine phosphorylation was prevented by genistein, a tyrosine kinase inhibitor. The site of tyrosine phosphorylation was identified on Tyr-10 by controlled trypsinolysis in rat PCTs and by site-directed mutagenesis in opossum kidney cells transfected with rat alpha-subunit. The functional relevance of Tyr-10 phosphorylation was assessed by 1) the abolition of insulin-induced stimulation of the ouabain-sensitive (86)Rb uptake in opossum kidney cells expressing mutant rat alpha1-subunits wherein tyrosine was replaced by alanine or glutamine; and 2) the similarity of the time course and dose dependency of the insulin-induced increase in ouabain-sensitive (86)Rb uptake and tyrosine phosphorylation. These findings indicate that phosphorylation of the Na+,K(+)-ATPase alpha-subunit at Tyr-10 likely participates in the physiological control of sodium reabsorption in PCT.
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