ArticleThe Journal of biological chemistry2011
Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 126 citations in OpenAlex.
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- MZB1-Driven Endoplasmic reticulum stress model as a predictor of breast cancer progression and survival.Functional & integrative genomics · 2025Article
- Selenoprotein K Is a Peripheral ER Membrane Protein.Biochemistry · 2025Article
- Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025Review
- Inferring post-transcriptional regulation within and across cell types in human testis.bioRxiv : the preprint server for biology · 2024Article
- Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023Review
- "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023Review
- Different Dietary Sources of Selenium Alleviate Hepatic Lipid Metabolism Disorder of Heat-Stressed Broilers by Relieving Endoplasmic Reticulum Stress.International journal of molecular sciences · 2023Article
- Selenoprotein S Interacts with the Replication and Transcription Complex of SARS-CoV-2 by Binding nsp7.Journal of molecular biology · 2023Article
- Effects of Selenoprotein S Knockdown on Endoplasmic Reticulum Stress in ATDC5 Cells and Gene Expression Profiles in Hypertrophic Chondrocytes.Biological trace element research · 2023Article
- Selenoprotein K enhances STING oligomerization to facilitate antiviral response.PLoS pathogens · 2023Article
- Molecular Mechanisms of the Cytotoxic Effect of Recombinant Selenoprotein SELENOM on Human Glioblastoma Cells.International journal of molecular sciences · 2023Article
- Noncanonical Form of ERAD Regulates Cardiac Hypertrophy.Circulation · 2023Article
- An arrayed CRISPR screen of primary B cells reveals the essential elements of the antibody secretion pathway.Frontiers in immunology · 2023Article
- Selenium in Bodily Homeostasis: Hypothalamus, Hormones, and Highways of Communication.International journal of molecular sciences · 2022Review
- Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022Review
- Selenium and Selenoproteins at the Intersection of Type 2 Diabetes and Thyroid Pathophysiology.Antioxidants (Basel, Switzerland) · 2022Review
- Article
- Selenoprotein K protects skeletal muscle from damage and is required for satellite cells-mediated myogenic differentiation.Redox biology · 2022Article
- Selenoprotein K deficiency-induced apoptosis: A role for calpain and the ERS pathway.Redox biology · 2021Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Selenoprotein K (SelK) is an 11-kDa endoplasmic reticulum (ER) protein of unknown function. Herein, we defined a new eukaryotic protein family that includes SelK, selenoprotein S (SelS), and distantly related proteins. Comparative genomics analyses indicate that this family is the most widespread eukaryotic selenoprotein family. A biochemical search for proteins that interact with SelK revealed ER-associated degradation (ERAD) components (p97 ATPase, Derlins, and SelS). In this complex, SelK showed higher affinity for Derlin-1, whereas SelS had higher affinity for Derlin-2, suggesting that these selenoproteins could determine the nature of the substrate translocated through the Derlin channel. SelK co-precipitated with soluble glycosylated ERAD substrates and was involved in their degradation. Its gene contained a functional ER stress response element, and its expression was up-regulated by conditions that induce the accumulation of misfolded proteins in the ER. Components of the oligosaccharyltransferase complex (ribophorins, OST48, and STT3A) and an ER chaperone, calnexin, were found to bind SelK. A glycosylated form of SelK was also detected, reflecting its association with the oligosaccharyltransferase complex. These data suggest that SelK is involved in the Derlin-dependent ERAD of glycosylated misfolded proteins and that the function defined by the prototypic SelK is the widespread function of selenium in eukaryotes.
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