ArticleProceedings of the National Academy of Sciences of the United States of America2020
Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 68 citations in OpenAlex.
- Mitochondria-endoplasmic reticulum-lipid droplet crosstalk in lipid metabolic reprogramming in type 2 diabetes mellitus.Journal of lipid research · 2026Review
- ER proteostasis meets mitochondrial function: contact sites as hubs of communication and therapeutic targets.The FEBS journal · 2026Review
- Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026Review
- Selenium in the Preterm Infant: Are We Supplementing Enough in This Vulnerable Population?Nutrients · 2026Review
- Endoplasmic reticulum stress in disease pathogenesis: its implications for therapy.Signal transduction and targeted therapy · 2026Review
- Genetics of selenoproteins and selenoprotein metabolism - An overview of current concepts and emerging aspects.Redox biology · 2026Review
- Tracing the vertebrate selenoproteome evolution reveals expansions in ray-finned fishes and convergent depletions in tetrapods.BMC genomics · 2026Article
- Selenium-Biofortified Probiotics: A Synergistic Microbial-Nutritional Strategy Against Exercise-Induced Stress.Nutrients · 2026Review
- Selenoprotein N and SEPN1-Related Myopathies: Mechanisms, Models, and Therapeutic Perspectives.Biomolecules · 2026Review
- Metabolic Functions and Mechanisms of Selenium, Selenocysteine, and GPX4 Mediated Immune Regulation Through Autophagy in Solid Tumors.Food science & nutrition · 2025Review
- Calcium dissociation with carbonate ions from Pf-SCP, sarcoplasmic calcium-binding protein in Pinctada fucata, contributes to calcium mineralization for shell formation.Protein science : a publication of the Protein Society · 2025Article
- Low Selenium Diet Inhibited CaMKII Activation via miR-365-3p/SelT Signaling Axis, Resulting in Myoblast Differentiation Disorders and Skeletal Muscle Damage in Broilers.Biological trace element research · 2025Article
- Selenium and Skeletal Muscle Health in Sports Nutrition.Nutrients · 2025Review
- Translational selenium nanomedicine synergizes with nab-paclitaxel to enhance antitumor effects in esophageal squamous cell cancer via selenoprotein N-mediated ER stress.Journal of nanobiotechnology · 2025Article
- Role of selenium in the pathophysiology of cardiorenal anaemia syndrome.ESC heart failure · 2025Review
- Zebrafish and cellular models of SELENON-Congenital myopathy exhibit novel embryonic and metabolic phenotypes.Skeletal muscle · 2025Article
- The Impact of Sodium Selenite and Seleno-L-Methionine on Stress Erythropoiesis in a Murine Model of Hemolytic Anemia.The Journal of nutrition · 2025Article
- Applying the algorithm for Proven and young in GWAS Reveals high polygenicity for key traits in Nellore cattle.Frontiers in genetics · 2025Article
- Development of a sensor to detect methylmercury toxicity.Scientific reports · 2024Article
- Impaired Upper Airway Muscle Function with Excessive or Deficient Dietary Intake of Selenium in Rats.Antioxidants (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
16 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum (ER) is the reservoir for calcium in cells. Luminal calcium levels are determined by calcium-sensing proteins that trigger calcium dynamics in response to calcium fluctuations. Here we report that Selenoprotein N (SEPN1) is a type II transmembrane protein that senses ER calcium fluctuations by binding this ion through a luminal EF-hand domain. In vitro and in vivo experiments show that via this domain, SEPN1 responds to diminished luminal calcium levels, dynamically changing its oligomeric state and enhancing its redox-dependent interaction with cellular partners, including the ER calcium pump sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCA). Importantly, single amino acid substitutions in the EF-hand domain of SEPN1 identified as clinical variations are shown to impair its calcium-binding and calcium-dependent structural changes, suggesting a key role of the EF-hand domain in SEPN1 function. In conclusion, SEPN1 is a ER calcium sensor that responds to luminal calcium depletion, changing its oligomeric state and acting as a reductase to refill ER calcium stores.
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