ArticleThe Journal of biological chemistry2013
Neutral phospholipids stimulate Na,K-ATPase activity: a specific lipid-protein interaction.
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 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Structural-functional aberrations of erythrocytes in the northern red-backed vole (Clethrionomys rutilus Pallas, 1779) that inhabits the zone of influence of the copper smelter (the Middle Ural).Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- The role of human milk fats in shaping neonatal development and the early life gut microbiota.Microbiome research reports · 2023Review
- Sequential purification and characterization of Torpedo californica nAChR-DC supplemented with CHS for high-resolution crystallization studies.Analytical biochemistry · 2020Article
- Overview on solubilization and lipid reconstitution of Na,K-ATPase: enzyme kinetic and biophysical characterization.Biophysical reviews · 2020Review
- 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 and the Safety Factor for Neuromuscular Transmission.International journal of molecular sciences · 2019Review
- AMP-Activated Protein Kinase as a Key Trigger for the Disuse-Induced Skeletal Muscle Remodeling.International journal of molecular sciences · 2018Review
- Renal Mg handling, FXYD2 and the central role of the Na,K-ATPase.Physiological reports · 2018Review
- Membrane lipid rafts are disturbed in the response of rat skeletal muscle to short-term disuse.American journal of physiology. Cell physiology · 2017Article
- Specific phospholipid binding to Na,K-ATPase at two distinct sites.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart: DISTINCT FUNCTIONAL PROPERTIES AND ISOFORM-SELECTIVE INHIBITORS.The Journal of biological chemistry · 2016Article
- Structural and Functional Basis for Lipid Synergy on the Activity of the Antibacterial Peptide ABC Transporter McjD.The Journal of biological chemistry · 2016Article
- Specialized Functional Diversity and Interactions of the Na,K-ATPase.Frontiers in physiology · 2016Review
- Membrane Lipid Microenvironment Modulates Thermodynamic Properties of the NaFrontiers in physiology · 2016Article
- Molecular Mechanisms and Kinetic Effects of FXYD1 and Phosphomimetic Mutants on Purified Human Na,K-ATPase.The Journal of biological chemistry · 2015Article
- Simulation of alcohol action upon a detailed Purkinje neuron model and a simpler surrogate model that runs >400 times faster.BMC neuroscience · 2015Article
- Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites.The Journal of biological chemistry · 2015Article
- Substrate recognition by the cell surface palmitoyl transferase DHHC5.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins interact with phospholipids either via an annular layer surrounding the transmembrane segments or by specific lipid-protein interactions. Although specifically bound phospholipids are observed in many crystal structures of membrane proteins, their roles are not well understood. Na,K-ATPase is highly dependent on acid phospholipids, especially phosphatidylserine, and previous work on purified detergent-soluble recombinant Na,K-ATPase showed that phosphatidylserine stabilizes and specifically interacts with the protein. Most recently the phosphatidylserine binding site has been located between transmembrane segments of αTM8-10 and the FXYD protein. This paper describes stimulation of Na,K-ATPase activity of the purified human α1β1 or α1β1FXYD1 complexes by neutral phospholipids, phosphatidylcholine, or phosphatidylethanolamine. In the presence of phosphatidylserine, soy phosphatidylcholine increases the Na,K-ATPase turnover rate from 5483 ± 144 to 7552 ± 105 (p < 0.0001). Analysis of α1β1FXYD1 complexes prepared with native or synthetic phospholipids shows that the stimulatory effect is structurally selective for neutral phospholipids with polyunsaturated fatty acyl chains, especially dilinoleoyl phosphatidylcholine or phosphatidylethanolamine. By contrast to phosphatidylserine, phosphatidylcholine or phosphatidylethanolamine destabilizes the Na,K-ATPase. Structural selectivity for stimulation of Na,K-ATPase activity and destabilization by neutral phospholipids distinguish these effects from the stabilizing effects of phosphatidylserine and imply that the phospholipids bind at distinct sites. A re-examination of electron densities of shark Na,K-ATPase is consistent with two bound phospholipids located between transmembrane segments αTM8-10 and TMFXYD (site A) and between TM2, -4, -6, -and 9 (site B). Comparison of the phospholipid binding pockets in E2 and E1 conformations suggests a possible mechanism of stimulation of Na,K-ATPase activity by the neutral phospholipid.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.