ArticleBiochimica et biophysica acta2009
Effects of PKA phosphorylation on the conformation of the Na,K-ATPase regulatory protein FXYD1.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Role of NaInternational journal of molecular sciences · 2024Review
- Identified and potential internalization signals involved in trafficking and regulation of NaMolecular and cellular biochemistry · 2024Review
- Structural basis for allosteric control of the SERCA-Phospholamban membrane complex by CaeLife · 2021Article
- Protein docking and steered molecular dynamics suggest alternative phospholamban-binding sites on the SERCA calcium transporter.The Journal of biological chemistry · 2020Article
- Review
- Polyamines regulate phosphorylation-dephosphorylation kinetics in a crustacean gill (NaMolecular and cellular biochemistry · 2017Article
- Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines.Biochimica et biophysica acta · 2015Article
- Mild hyperhomocysteinemia reduces the activity and immunocontent, but does not alter the gene expression, of catalytic α subunits of cerebral Na+,K+-ATPase.Molecular and cellular biochemistry · 2013Article
- Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.Journal of biomolecular NMR · 2013Article
- Regulation of the cardiac sodium pump.Cellular and molecular life sciences : CMLS · 2013Review
- The inhibitory effect of phospholemman on the sodium pump requires its palmitoylation.The Journal of biological chemistry · 2011Article
- Phospholamban binds with differential affinity to calcium pump conformers.The Journal of biological chemistry · 2011Article
- Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase.The Journal of biological chemistry · 2011Article
- Phospholemman: a novel cardiac stress protein.Clinical and translational science · 2010Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
FXYD1 (phospholemman) is a member of an evolutionarily conserved family of membrane proteins that regulate the function of the Na,K-ATPase enzyme complex in specific tissues and specific physiological states. In heart and skeletal muscle sarcolemma, FXYD1 is also the principal substrate of hormone-regulated phosphorylation by c-AMP dependent protein kinase A and by protein kinase C, which phosphorylate the protein at conserved Ser residues in its cytoplasmic domain, altering its Na,K-ATPase regulatory activity. FXYD1 adopts an L-shaped alpha-helical structure with the transmembrane helix loosely connected to a cytoplasmic amphipathic helix that rests on the membrane surface. In this paper we describe NMR experiments showing that neither PKA phosphorylation at Ser68 nor the physiologically relevant phosphorylation mimicking mutation Ser68Asp induces major changes in the protein conformation. The results, viewed in light of a model of FXYD1 associated with the Na,K-ATPase alpha and beta subunits, indicate that the effects of phosphorylation on the Na,K-ATPase regulatory activity of FXYD1 could be due primarily to changes in electrostatic potential near the membrane surface and near the Na(+)/K(+) ion binding site of the Na,K-ATPase alpha subunit.
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Registered trials
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