ArticleThe Journal of biological chemistry2012
Protein kinase A (PKA) phosphorylation of Na+/K+-ATPase opens intracellular C-terminal water pathway leading to third Na+-binding site in molecular dynamics simulations.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Na+/K+-ATPase: a multifunctional target in type 2 diabetes and pancreatic islets.Frontiers in immunology · 2025Review
- ATP1A1-linked diseases require a malfunctioning protein product from one allele.Biochimica et biophysica acta. Molecular cell research · 2024Article
- Melatonin integrates multidimensional regulation of NaFrontiers in physiology · 2022Article
- Protein Kinase C Mediates the Corticosterone-induced Sensitization of Dorsal Root Ganglion Neurons Innervating the Rat Stomach.Journal of neurogastroenterology and motility · 2017Article
- Glutamate Water Gates in the Ion Binding Pocket of NaScientific reports · 2017Article
- Importance of a Potential Protein Kinase A Phosphorylation Site of Na+,K+-ATPase and Its Interaction Network for Na+ Binding.The Journal of biological chemistry · 2016Article
- A novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study.BMC bioinformatics · 2016Article
- Phosphorylation of rat kidney Na-K pump at Ser938 is required for rapid angiotensin II-dependent stimulation of activity and trafficking in proximal tubule cells.American journal of physiology. Cell physiology · 2016Article
- Physicochemical mechanisms of protein regulation by phosphorylation.Frontiers in genetics · 2014Review
- Microsecond molecular dynamics simulations of Mg²⁺- and K⁺-bound E1 intermediate states of the calcium pump.PloS one · 2014Article
- PharmGKB summary: Diuretics pathway, pharmacodynamics.Pharmacogenetics and genomics · 2013Article
- Protein kinase-dependent oxidative regulation of the cardiac Na+-K+ pump: evidence from in vivo and in vitro modulation of cell signalling.The Journal of physiology · 2013Article
- A specific and essential role for Na,K-ATPase α3 in neurons co-expressing α1 and α3.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation is one of the major mechanisms for posttranscriptional modification of proteins. The addition of a compact, negatively charged moiety to a protein can significantly change its function and localization by affecting its structure and interaction network. We have used all-atom Molecular Dynamics simulations to investigate the structural consequences of phosphorylating the Na(+)/K(+)-ATPase (NKA) residue Ser(936), which is the best characterized phosphorylation site in NKA, targeted in vivo by protein kinase A (PKA). The Molecular Dynamics simulations suggest that Ser(936) phosphorylation opens a C-terminal hydrated pathway leading to Asp(926), a transmembrane residue proposed to form part of the third sodium ion-binding site. Simulations of a S936E mutant form, for which only subtle effects are observed when expressed in Xenopus oocytes and studied with electrophysiology, does not mimic the effects of Ser(936) phosphorylation. The results establish a structural association of Ser(936) with the C terminus of NKA and indicate that phosphorylation of Ser(936) can modulate pumping activity by changing the accessibility to the ion-binding site.
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