ArticleThe Journal of biological chemistry2013
Expression of mutant α1 Na/K-ATPase defective in conformational transition attenuates Src-mediated signal transduction.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Factors that influence the Na/K-ATPase signaling and function.Frontiers in pharmacology · 2025Review
- Role of Na/K-ATPase α1 caveolin-binding motif in adipogenesis.American journal of physiology. Cell physiology · 2024Article
- The vascular Na,K-ATPase: clinical implications in stroke, migraine, and hypertension.Clinical science (London, England : 1979) · 2023Review
- In Vitro Study of the Multimodal Effect of NaBiomedicines · 2023Article
- The microtubule network enables Src kinase interaction with the Na,K-ATPase to generate CaFrontiers in physiology · 2022Article
- The Na/K-ATPase α1/Src interaction regulates metabolic reserve and Western diet intolerance.Acta physiologica (Oxford, England) · 2021Article
- Inverse agonism at the Na/K-ATPase receptor reverses EMT in prostate cancer cells.The Prostate · 2021Article
- Biased Effect of Cardiotonic Steroids on Na/K-ATPase-Mediated Signal Transduction.Molecular pharmacology · 2021Article
- Anticancer and Antiviral Properties of Cardiac Glycosides: A Review to Explore the Mechanism of Actions.Molecules (Basel, Switzerland) · 2020Review
- A caveolin binding motif in Na/K-ATPase is required for stem cell differentiation and organogenesis in mammals andScience advances · 2020Article
- The Flot2 component of the lipid raft changes localization during neural differentiation of P19C6 cells.BMC molecular and cell biology · 2019Article
- Smooth muscle CaJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2019Article
- Effect of photobiomodulation therapy on neuronal injuries by ouabain: the regulation of Na, K-ATPase; Src; and mitogen-activated protein kinase signaling pathway.BMC neuroscience · 2019Article
- Oleandrin and Its Derivative Odoroside A, Both Cardiac Glycosides, Exhibit Anticancer Effects by Inhibiting Invasion via Suppressing the STAT-3 Signaling Pathway.International journal of molecular sciences · 2018Review
- The Na,K-ATPase-Dependent Src Kinase Signaling Changes with Mesenteric Artery Diameter.International journal of molecular sciences · 2018Article
- Na/K-ATPase Y260 Phosphorylation-mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth.Scientific reports · 2018Article
- Heterogeneity of signal transduction by Na-K-ATPase α-isoforms: role of Src interaction.American journal of physiology. Cell physiology · 2018Article
- Protein Interaction and Na/K-ATPase-Mediated Signal Transduction.Molecules (Basel, Switzerland) · 2017Review
- Na/K Pump and Beyond: Na/K-ATPase as a Modulator of Apoptosis and Autophagy.Molecules (Basel, Switzerland) · 2017Review
- Na⁺Molecules (Basel, Switzerland) · 2017Review
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Authors and funding
7 authors.
Funding
Abstract
The α1 Na/K-ATPase possesses both pumping and signaling functions. Using purified enzyme we found that the α1 Na/K-ATPase might interact with and regulate Src activity in a conformation-dependent manner. Here we further explored the importance of the conformational transition capability of α1 Na/K-ATPase in regulation of Src-related signal transduction in cell culture. We first rescued the α1-knockdown cells by wild-type rat α1 or α1 mutants (I279A and F286A) that are known to be defective in conformational transition. Stable cell lines with comparable expression of wild type α1, I279A, and F286A were characterized. As expected, the defects in conformation transition resulted in comparable degree of inhibition of pumping activity in the mutant-rescued cell lines. However, I279A was more effective in inhibiting basal Src activity than either the wild-type or the F286A. Although much higher ouabain concentration was required to stimulate Src in I279A-rescued cells, extracellular K(+) was comparably effective in regulating Src in both control and I279A cells. In contrast, ouabain and extracellular K(+) failed to produce detectable changes in Src activity in F286A-rescued cells. Furthermore, expression of either mutant inhibited integrin-induced activation of Src/FAK pathways and slowed cell spreading processes. Finally, the expression of these mutants inhibited cell growth, with I279A being more potent than that of F286A. Taken together, the new findings suggest that the α1 Na/K-ATPase may be a key player in dynamic regulation of cellular Src activity and that the capability of normal conformation transition is essential for both pumping and signaling functions of α1 Na/K-ATPase.
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