ArticleThe Journal of membrane biology2006
The third sodium binding site of Na,K-ATPase is functionally linked to acidic pH-activated inward current.
Article in The Journal of membrane biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- NaFrontiers in chemistry · 2026Article
- Displacement of the NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- A novel ATP1A2 mutation in a patient with hypokalaemic periodic paralysis and CNS symptoms.Brain : a journal of neurology · 2018Article
- The CAPOS mutation in ATP1A3 alters Na/K-ATPase function and results in auditory neuropathy which has implications for management.Human genetics · 2018Article
- On the effect of hyperaldosteronism-inducing mutations in Na/K pumps.The Journal of general physiology · 2017Article
- Molecular simulations and free-energy calculations suggest conformation-dependent anion binding to a cytoplasmic site as a mechanism for NaThe Journal of biological chemistry · 2017Article
- Glutamate Water Gates in the Ion Binding Pocket of NaScientific reports · 2017Article
- Intracellular Requirements for Passive Proton Transport through the NaBiophysical journal · 2016Article
- Article
- ATP1A2 Mutations in Migraine: Seeing through the Facets of an Ion Pump onto the Neurobiology of Disease.Frontiers in physiology · 2016Review
- Sodium and proton effects on inward proton transport through Na/K pumps.Biophysical journal · 2014Article
- Route, mechanism, and implications of proton import during Na+/K+ exchange by native Na+/K+-ATPase pumps.The Journal of general physiology · 2014Article
- Fishing for holes in transporters: how protons breach the Na/K pump security gates.The Journal of general physiology · 2014Article
- A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps.Nature reviews. Molecular cell biology · 2011Review
- Selectivity of externally facing ion-binding sites in the Na/K pump to alkali metals and organic cations.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Neurological disease mutations compromise a C-terminal ion pathway in the Na(+)/K(+)-ATPase.Nature · 2010Article
- The rapid-onset dystonia parkinsonism mutation D923N of the Na+, K+-ATPase alpha3 isoform disrupts Na+ interaction at the third Na+ site.The Journal of biological chemistry · 2010Article
- The two C-terminal tyrosines stabilize occluded Na/K pump conformations containing Na or K ions.The Journal of general physiology · 2010Article
- Hyperpolarization-activated inward leakage currents caused by deletion or mutation of carboxy-terminal tyrosines of the Na+/K+-ATPase {alpha} subunit.The Journal of general physiology · 2010Article
- Altered Na+ transport after an intracellular alpha-subunit deletion reveals strict external sequential release of Na+ from the Na/K pump.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sodium- and potassium-activated adenosine triphosphatases (Na,K-ATPase) is the ubiquitous active transport system that maintains the Na(+) and K(+) gradients across the plasma membrane by exchanging three intracellular Na(+) ions against two extracellular K(+) ions. In addition to the two cation binding sites homologous to the calcium site of sarcoplasmic and endoplasmic reticulum calcium ATPase and which are alternatively occupied by Na(+) and K(+) ions, a third Na(+)-specific site is located close to transmembrane domains 5, 6 and 9, and mutations close to this site induce marked alterations of the voltage-dependent release of Na(+) to the extracellular side. In the absence of extracellular Na(+) and K(+), Na,K-ATPase carries an acidic pH-activated, ouabain-sensitive "leak" current. We investigated the relationship between the third Na(+) binding site and the pH-activated current. The decrease (in E961A, T814A and Y778F mutants) or the increase (in G813A mutant) of the voltage-dependent extracellular Na(+) affinity was paralleled by a decrease or an increase in the pH-activated current, respectively. Moreover, replacing E961 with oxygen-containing side chain residues such as glutamine or aspartate had little effect on the voltage-dependent affinity for extracellular Na(+) and produced only small effects on the pH-activated current. Our results suggest that extracellular protons and Na(+) ions share a high field access channel between the extracellular solution and the third Na(+) binding site.
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