ArticleProceedings of the National Academy of Sciences of the United States of America2002
Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
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Who cites it
109 citing papers in PubMed, 270 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
- Effect of dexamethasone on skeletal muscle Na+,K+ pump subunit specific expression and K+ homeostasis during exercise in humans.The Journal of physiology · 2008Trial
- Spatial proteomics identifies FXYD6 as a dual-site protein of neuromuscular junction in the diaphragm.Communications biology · 2026Article
- 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
- Molecular Basis of Na, K-ATPase Regulation of Diseases: Hormone and FXYD2 Interactions.International journal of molecular sciences · 2024Review
- Role of NaInternational journal of molecular sciences · 2024Review
- AMPK and glucose deprivation exert an isoform-specific effect on the expression of NaJournal of muscle research and cell motility · 2024Article
- Effects of conceptus proteins on endometrium and blood leukocytes of dairy cattle using transcriptome and meta-analysis.bioRxiv : the preprint server for biology · 2024Article
- A century of exercise physiology: effects of muscle contraction and exercise on skeletal muscle NaEuropean journal of applied physiology · 2024Review
- Data-Independent Acquisition Proteomics and N-Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts.Journal of proteome research · 2024Article
- Small but mighty: the rise of microprotein biology in neuroscience.Frontiers in molecular neuroscience · 2024Article
- The zebrafish mutanteLife · 2023Article
- Hypoxic Stress-Dependent Regulation of Na,K-ATPase in Ischemic Heart Disease.International journal of molecular sciences · 2023Review
- High-Intensity Training Represses FXYD5 and Glycosylates Na,K-ATPase in Type II Muscle Fibres, Which Are Linked with Improved Muscle KInternational journal of molecular sciences · 2023Article
- The role of NaCNS neuroscience & therapeutics · 2022Review
- The cardiac-enriched microprotein mitolamban regulates mitochondrial respiratory complex assembly and function in mice.Proceedings of the National Academy of Sciences of the United States of America · 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
- The role of AMPK in regulation of NaJournal of muscle research and cell motility · 2021Review
49 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A family of small, single-span membrane proteins (the FXYD family) has recently been defined based on their sequence and structural homology. Some members of this family have already been identified as tissue-specific regulators of Na,K-ATPase (NKA). In the present study, we demonstrate that phospholemman (PLM) (FXYD1), so far considered to be a heart- and muscle-specific channel or channel-regulating protein, associates specifically and stably with six different alpha-beta isozymes of NKA after coexpression in Xenopus oocytes, and with alpha1-beta, and less efficiently with alpha2-beta isozymes, in native cardiac and skeletal muscles. Stoichiometric association of PLM with NKA occurs posttranslationally either in the Golgi or the plasma membrane. Interaction of PLM with NKA induces a small decrease in the external K+ affinity of alpha1-beta1 and alpha2-beta1 isozymes and a nearly 2-fold decrease in the internal Na+ affinity. In conclusion, this study demonstrates that PLM is a tissue-specific regulator of NKA that may play an essential role in muscle contractility.
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Registered trials
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.