ArticleThe Journal of biological chemistry2015
Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 79 citations in OpenAlex.
- Active conformations of neuronal NaNature communications · 2026Article
- Gangliosides in molecular interactions and cell regulation.The Journal of biological chemistry · 2026Review
- Signal Strength Aware Latent Spaces Reveal Molecularly Distinct Substructures within Human Kidney Tissue.bioRxiv : the preprint server for biology · 2026Article
- Review
- A lipid atlas of the human kidney.Science advances · 2025Article
- Current Targets and Future Directions of Positive Inotropes for Heart Failure.Current medicinal chemistry · 2024Review
- Electrostatic switch mechanisms of membrane protein trafficking and regulation.Biophysical reviews · 2023Review
- Short-Term Mild Hypoxia Modulates Na,K-ATPase to Maintain Membrane Electrogenesis in Rat Skeletal Muscle.International journal of molecular sciences · 2022Article
- mPPases create a conserved anionic membrane fingerprint as identified via multi-scale simulations.PLoS computational biology · 2022Article
- Possible Role of Extracellular Vesicles in Hepatotoxicity of Acetaminophen.International journal of molecular sciences · 2022Article
- Start Me Up: How Can Surrounding Gangliosides Affect Sodium-Potassium ATPase Activity and Steer towards Pathological Ion Imbalance in Neurons?Biomedicines · 2022Review
- Sterol Extraction from Isolated Plant Plasma Membrane Vesicles Affects HBiomolecules · 2021Article
- Evaluation of Cardiotonic Steroid Modulation of Cellular Cholesterol and Phospholipid.The Journal of membrane biology · 2021Article
- Effect of Detergents on Activity and Magnesium-Dependent Properties of Different Isoforms of NaBulletin of experimental biology and medicine · 2021Article
- Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021Review
- Evaluation of the Erythrocyte Membrane in Head and Neck Cancer Patients.The Journal of membrane biology · 2020Article
- Capturing Biologically Complex Tissue-Specific Membranes at Different Levels of Compositional Complexity.The journal of physical chemistry. B · 2020Article
- General and specific interactions of the phospholipid bilayer with P-type ATPases.Biophysical reviews · 2019Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Cholesterol depletion inhibits NaThe Journal of biological chemistry · 2019Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of membrane proteins such as Na,K-ATPase depends strongly on the surrounding lipid environment. Interactions can be annular, depending on the physical properties of the membrane, or specific with lipids bound in pockets between transmembrane domains. This paper describes three specific lipid-protein interactions using purified recombinant Na,K-ATPase. (a) Thermal stability of the Na,K-ATPase depends crucially on a specific interaction with 18:0/18:1 phosphatidylserine (1-stearoyl-2-oleoyl-sn-glycero-3-phospho-L-serine; SOPS) and cholesterol, which strongly amplifies stabilization. We show here that cholesterol associates with SOPS, FXYD1, and the α subunit between trans-membrane segments αTM8 and -10 to stabilize the protein. (b) Polyunsaturated neutral lipids stimulate Na,K-ATPase turnover by >60%. A screen of the lipid specificity showed that 18:0/20:4 and 18:0/22:6 phosphatidylethanolamine (PE) are the optimal phospholipids for this effect. (c) Saturated phosphatidylcholine and sphingomyelin, but not saturated phosphatidylserine or PE, inhibit Na,K-ATPase activity by 70-80%. This effect depends strongly on the presence of cholesterol. Analysis of the Na,K-ATPase activity and E1-E2 conformational transitions reveals the kinetic mechanisms of these effects. Both stimulatory and inhibitory lipids poise the conformational equilibrium toward E2, but their detailed mechanisms of action are different. PE accelerates the rate of E1 → E2P but does not affect E2(2K)ATP → E13NaATP, whereas sphingomyelin inhibits the rate of E2(2K)ATP → E13NaATP, with very little effect on E1 → E2P. We discuss these lipid effects in relation to recent crystal structures of Na,K-ATPase and propose that there are three separate sites for the specific lipid interactions, with potential physiological roles to regulate activity and stability of the pump.
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