ArticleProceedings of the National Academy of Sciences of the United States of America2009
Altered Na+ transport after an intracellular alpha-subunit deletion reveals strict external sequential release of Na+ from the Na/K pump.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- On the mechanism of hypomagnesemia with treatment-resistant seizures caused by variants of the Na+,K+-ATPase α1 subunit (ATP1A1).The Journal of general physiology · 2026Article
- Structure and function of HNature communications · 2022Article
- Role of a conserved ion-binding site tyrosine in ion selectivity of the Na+/K+ pump.The Journal of general physiology · 2022Article
- Displacement of the NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- FXYD protein isoforms differentially modulate human Na/K pump function.The Journal of general physiology · 2020Article
- Functional consequences of the CAPOS mutation E818K of NaThe Journal of biological chemistry · 2019Article
- External Ion Access in the Na/K Pump: Kinetics of NaBiophysical journal · 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
- Arginine substitution of a cysteine in transmembrane helix M8 converts Na+,K+-ATPase to an electroneutral pump similar to H+,K+-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Intracellular Requirements for Passive Proton Transport through the NaBiophysical journal · 2016Article
- ATP1A2 Mutations in Migraine: Seeing through the Facets of an Ion Pump onto the Neurobiology of Disease.Frontiers in physiology · 2016Review
- Importance of the Voltage Dependence of Cardiac Na/K ATPase Isozymes.Biophysical journal · 2015Article
- K+ congeners that do not compromise Na+ activation of the Na+,K+-ATPase: hydration of the ion binding cavity likely controls ion selectivity.The Journal of biological chemistry · 2015Article
- Sodium and proton effects on inward proton transport through Na/K pumps.Biophysical journal · 2014Article
- Functional analysis of human Na(+)/K(+)-ATPase familial or sporadic hemiplegic migraine mutations expressed in Xenopus oocytes.World journal of biological chemistry · 2014Article
- Route, mechanism, and implications of proton import during Na+/K+ exchange by native Na+/K+-ATPase pumps.The Journal of general physiology · 2014Article
- Relationship between intracellular Na+ concentration and reduced Na+ affinity in Na+,K+-ATPase mutants causing neurological disease.The Journal of biological chemistry · 2014Article
- Ionic leakage underlies a gain-of-function effect of dominant disease mutations affecting diverse P-type ATPases.Nature genetics · 2014Article
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4 authors.
Funding
Abstract
The Na/K pump actively exports 3 Na(+) in exchange for 2 K(+) across the plasmalemma of animal cells. As in other P-type ATPases, pump function is more effective when the relative affinity for transported ions is altered as the ion binding sites alternate between opposite sides of the membrane. Deletion of the five C-terminal residues from the alpha-subunit diminishes internal Na(+) (Na(i)(+)) affinity approximately 25-fold [Morth et al. (2007) Nature 450:1043-1049]. Because external Na(+) (Na(o)(+)) binding is voltage-dependent, we studied the reactions involving this process by using two-electrode and inside-out patch voltage clamp in normal and truncated (DeltaKESYY) Xenopus-alpha1 pumps expressed in oocytes. We observed that DeltaKESYY (i) decreased both Na(o)(+) and Na(i)(+) apparent affinities in the absence of K(o)(+), and (ii) did not affect apparent Na(o)(+) affinity at high K(o)(+). These results support a model of strict sequential external release of Na(+) ions, where the Na(+)-exclusive site releases Na(+) before the sites shared with K(+) and the DeltaKESYY deletion only reduces Na(o)(+) affinity at the shared sites. Moreover, at nonsaturating K(o)(+), DeltaKESYY induced an inward flow of Na(+) through Na/K pumps at negative potentials. Guanidinium(+) can also permeate truncated pumps, whereas N-methyl-D-glucamine cannot. Because guanidinium(o)(+) can also traverse normal Na/K pumps in the absence of both Na(o)(+) and K(o)(+) and can also inhibit Na/K pump currents in a Na(+)-like voltage-dependent manner, we conclude that the normal pathway transited by the first externally released Na(+) is large enough to accommodate guanidinium(+).
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