ArticleThe Journal of biological chemistry2016
Do Src Kinase and Caveolin Interact Directly with Na,K-ATPase?
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Article
- Na,K-ATPase mediated and cardiotonic induced signaling in health and disease.Frontiers in physiology · 2025Review
- Factors that influence the Na/K-ATPase signaling and function.Frontiers in pharmacology · 2025Review
- Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024Review
- The vascular Na,K-ATPase: clinical implications in stroke, migraine, and hypertension.Clinical science (London, England : 1979) · 2023Review
- Article
- The microtubule network enables Src kinase interaction with the Na,K-ATPase to generate CaFrontiers in physiology · 2022Article
- Alzheimer's Aβ assembly binds sodium pump and blocks endothelial NOS activity via ROS-PKC pathway in brain vascular endothelial cells.iScience · 2021Article
- A caveolin binding motif in Na/K-ATPase is required for stem cell differentiation and organogenesis in mammals andScience advances · 2020Article
- The Na/K-ATPase α1 and c-Src form signaling complex under native condition: A crosslinking approach.Scientific reports · 2020Article
- Overview on solubilization and lipid reconstitution of Na,K-ATPase: enzyme kinetic and biophysical characterization.Biophysical reviews · 2020Review
- Energy and Dynamics of Caveolae Trafficking.Frontiers in cell and developmental biology · 2020Review
- The sodium pump and digitalis drugs: Dogmas and fallacies.Pharmacology research & perspectives · 2019Review
- Smooth muscle CaJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2019Article
- The Na/K-ATPase Signaling: From Specific Ligands to General Reactive Oxygen Species.International journal of molecular sciences · 2018Review
- Quantum Modeling: A Bridge between the Pumping and Signaling Functions of Na/K-ATPase.International journal of molecular sciences · 2018Article
- Na/K-ATPase/src complex mediates regulation of CD40 in renal parenchyma.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2018Article
- Heterogeneity of signal transduction by Na-K-ATPase α-isoforms: role of Src interaction.American journal of physiology. Cell physiology · 2018Article
- Targeting Na/K-ATPase Signaling: A New Approach to Control Oxidative Stress.Current pharmaceutical design · 2018Review
- Gestation changes sodium pump isoform expression, leading to changes in ouabain sensitivity, contractility, and intracellular calcium in rat uterus.Physiological reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Much evidence points to a role of Na,K-ATPase in ouabain-dependent signal transduction. Based on experiments with different cell lines and native tissue membranes, a current hypothesis postulates direct interactions between the Na,K-ATPase and Src kinase (non-receptor tyrosine kinase). Na,K-ATPase is proposed to bind Src kinase and inhibit its activity, whereas ouabain, the specific Na,K-ATPase inhibitor, binds and stabilizes the E2 conformation, thus exposing the Src kinase domain and its active site Tyr-418 for activation. Ouabain-dependent signaling is thought to be mediated within caveolae by a complex consisting of Na,K-ATPase, caveolin, and Src kinase. In the current work, we have looked for direct interactions utilizing purified recombinant Na,K-ATPase (human α1β1FXYD1 or porcine α1D369Nβ1FXYD1) and purified human Src kinase and human caveolin 1 or interactions between these proteins in native membrane vesicles isolated from rabbit kidney. By several independent criteria and techniques, no stable interactions were detected between Na,K-ATPase and purified Src kinase. Na,K-ATPase was found to be a substrate for Src kinase phosphorylation at Tyr-144. Clear evidence for a direct interaction between purified human Na,K-ATPase and human caveolin was obtained, albeit with a low molar stoichiometry (1:15-30 caveolin 1/Na,K-ATPase). In native renal membranes, a specific caveolin 14-5 oligomer (95 kDa) was found to be in direct interaction with Na,K-ATPase. We inferred that a small fraction of the renal Na,K-ATPase molecules is in a ∼1:1 complex with a caveolin 14-5 oligomer. Thus, overall, whereas a direct caveolin 1/Na,K-ATPase interaction is confirmed, the lack of direct Src kinase/Na,K-ATPase binding requires reassessment of the mechanism of ouabain-dependent signaling.
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