ArticleEMBO reports2017
Selenoprotein T is a novel OST subunit that regulates UPR signaling and hormone secretion.
Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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
29 citing papers in PubMed, 57 citations in OpenAlex.
- Harnessing the novel safeguarding role of Selenoprotein T in age-related myocardial left and right decline through the ferroptosis-mitochondrial axis.Journal of translational medicine · 2026Article
- Unveiling Selenoprotein T as a novel regulator of cardiomyocyte senescence: pivotal role of the CD36 receptor in AC16 human cardiomyocytes.GeroScience · 2026Article
- Central SELENOT deficiency impairs gonadotrope axis function, sexual behavior, and fertility in male and female mice.JCI insight · 2025Article
- The selenocysteine-containing protein SELENOT maintains dopamine signaling in the midbrain to protect mice from hyperactivity disorder.The EMBO journal · 2025Article
- "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023Review
- "Alphabet" Selenoproteins: Implications in Pathology.International journal of molecular sciences · 2023Review
- Selenium in Prostate Cancer: Prevention, Progression, and Treatment.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Article
- Selenium in Bodily Homeostasis: Hypothalamus, Hormones, and Highways of Communication.International journal of molecular sciences · 2022Review
- The SELENOT mimetic PSELT promotes nerve regeneration by increasing axonal myelination in a facial nerve injury model in female rats.Journal of neuroscience research · 2022Article
- Selenoprotein K Is Essential for the Migration and Phagocytosis of Immature Dendritic Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Article
- Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022Review
- The Antioxidant Selenoprotein T Mimetic, PSELT, Induces Preconditioning-like Myocardial Protection by Relieving Endoplasmic-Reticulum Stress.Antioxidants (Basel, Switzerland) · 2022Article
- Mechanisms of the Cytotoxic Effect of Selenium Nanoparticles in Different Human Cancer Cell Lines.International journal of molecular sciences · 2021Article
- THE MAIN CYTOTOXIC EFFECTS OF METHYLSELENINIC ACID ON VARIOUS CANCER CELLS.International journal of molecular sciences · 2021Review
- Selenium, Selenoproteins, and Heart Failure: Current Knowledge and Future Perspective.Current heart failure reports · 2021Review
- The glyco-redox interplay: Principles and consequences on the role of reactive oxygen species during protein glycosylation.Redox biology · 2021Review
- Cell-penetrating, antioxidant SELENOT mimetic protects dopaminergic neurons and ameliorates motor dysfunction in Parkinson's disease animal models.Redox biology · 2021Article
- Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenoprotein T (SelT) is a recently characterized thioredoxin-like protein whose expression is very high during development, but is confined to endocrine tissues in adulthood where its function is unknown. We report here that SelT is required for adaptation to the stressful conditions of high hormone level production in endocrine cells. Using immunofluorescence and TEM immunogold approaches, we find that SelT is expressed at the endoplasmic reticulum membrane in all hormone-producing pituitary cell types. SelT knockdown in corticotrope cells promotes unfolded protein response (UPR) and ER stress and lowers endoplasmic reticulum-associated protein degradation (ERAD) and hormone production. Using a screen in yeast for SelT-membrane protein interactions, we sort keratinocyte-associated protein 2 (KCP2), a subunit of the protein complex oligosaccharyltransferase (OST). In fact, SelT interacts not only with KCP2 but also with other subunits of the A-type OST complex which are depleted after SelT knockdown leading to POMC N-glycosylation defects. This study identifies SelT as a novel subunit of the A-type OST complex, indispensable for its integrity and for ER homeostasis, and exerting a pivotal adaptive function that allows endocrine cells to properly achieve the maturation and secretion of hormones.
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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.