ArticleAmerican journal of physiology. Cell physiology2009
FXYD1 phosphorylation in vitro and in adult rat cardiac myocytes: threonine 69 is a novel substrate for protein kinase C.
Article in American journal of physiology. Cell physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 72 citations in OpenAlex.
- Intensive training and reduced volume increases muscle FXYD1 expression and phosphorylation at rest and during exercise in athletes.American journal of physiology. Regulatory, integrative and comparative physiology · 2016Trial
- The functions of FXYD family members in human health and disease.Genes & diseases · 2026Review
- Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications.Frontiers in cell and developmental biology · 2026Review
- Exercise- and diet-induced glycogen depletion impairs performance during one-legged constant-load, high-intensity exercise in humans.Frontiers in physiology · 2025Article
- ATP1A1-linked diseases require a malfunctioning protein product from one allele.Biochimica et biophysica acta. Molecular cell research · 2024Article
- Non-Selective PDE4 Inhibition Induces a Rapid and Transient Decrease of Serum Potassium in Mice.Biology · 2022Article
- Regulation of Cardiac Contractility by the Alpha 2 Subunit of the NaFrontiers in physiology · 2022Review
- FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021Review
- Phospholemman Phosphorylation Regulates Vascular Tone, Blood Pressure, and Hypertension in Mice and Humans.Circulation · 2021Article
- Design of a Proteolytically Stable Sodium-Calcium Exchanger 1 Activator Peptide forFrontiers in pharmacology · 2021Article
- FXYD protein isoforms differentially modulate human Na/K pump function.The Journal of general physiology · 2020Article
- Heart failure leads to altered β2-adrenoceptor/cyclic adenosine monophosphate dynamics in the sarcolemmal phospholemman/Na,K ATPase microdomain.Cardiovascular research · 2019Article
- Expression and regulation of type 2A protein phosphatases and alpha4 signalling in cardiac health and hypertrophy.Basic research in cardiology · 2017Article
- Impaired AQP2 trafficking in Fxyd1 knockout mice: A role for FXYD1 in regulated vesicular transport.PloS one · 2017Article
- Disulfide-activated protein kinase G Iα regulates cardiac diastolic relaxation and fine-tunes the Frank-Starling response.Nature communications · 2016Article
- Protein Phosphatase 1c Associated with the Cardiac Sodium Calcium Exchanger 1 Regulates Its Activity by Dephosphorylating Serine 68-phosphorylated Phospholemman.The Journal of biological chemistry · 2016Article
- "Oxygen Sensing" by Na,K-ATPase: These Miraculous Thiols.Frontiers in physiology · 2016Review
- Beneficial Renal and Pancreatic Phenotypes in a Mouse Deficient in FXYD2 Regulatory Subunit of Na,K-ATPase.Frontiers in physiology · 2016Review
- Molecular Mechanisms and Kinetic Effects of FXYD1 and Phosphomimetic Mutants on Purified Human Na,K-ATPase.The Journal of biological chemistry · 2015Article
- Importance of the Voltage Dependence of Cardiac Na/K ATPase Isozymes.Biophysical journal · 2015Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
FXYD1 (phospholemman), the primary sarcolemmal kinase substrate in the heart, is a regulator of the cardiac sodium pump. We investigated phosphorylation of FXYD1 peptides by purified kinases using HPLC, mass spectrometry, and Edman sequencing, and FXYD1 phosphorylation in cultured adult rat ventricular myocytes treated with PKA and PKC agonists by phosphospecific immunoblotting. PKA phosphorylates serines 63 and 68 (S63 and S68) and PKC phosphorylates S63, S68, and a new site, threonine 69 (T69). In unstimulated myocytes, FXYD1 is approximately 30% phosphorylated at S63 and S68, but barely phosphorylated at T69. S63 and S68 are rapidly dephosphorylated following acute inhibition of PKC in unstimulated cells. Receptor-mediated PKC activation causes sustained phosphorylation of S63 and S68, but transient phosphorylation of T69. To characterize the effect of T69 phosphorylation on sodium pump function, we measured pump currents using whole cell voltage clamping of cultured adult rat ventricular myocytes with 50 mM sodium in the patch pipette. Activation of PKA or PKC increased pump currents (from 2.1 +/- 0.2 pA/pF in unstimulated cells to 2.9 +/- 0.1 pA/pF for PKA and 3.4 +/- 0.2 pA/pF for PKC). Following kinase activation, phosphorylated FXYD1 was coimmunoprecipitated with sodium pump alpha(1)-subunit. We conclude that T69 is a previously undescribed phosphorylation site in FXYD1. Acute T69 phosphorylation elicits stimulation of the sodium pump additional to that induced by S63 and S68 phosphorylation.
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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.