ArticleBiochemistry2013
The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023Review
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- Selenoprotein S Interacts with the Replication and Transcription Complex of SARS-CoV-2 by Binding nsp7.Journal of molecular biology · 2023Article
- Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022Review
- Simiate and the focal adhesion kinase FAK1 cooperate in the regulation of dendritogenesis.Scientific reports · 2022Article
- Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity.Chemical science · 2022Article
- Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S.Methods in enzymology · 2022Article
- Diversity roles of CHD1L in normal cell function and tumorigenesis.Biomarker research · 2021Review
- Fis Connects Two Sensory Pathways, Quorum Sensing and Surface Sensing, to Control Motility inFrontiers in microbiology · 2021Article
- Role of Selenoproteins in Redox Regulation of Signaling and the Antioxidant System: A Review.Antioxidants (Basel, Switzerland) · 2020Review
- Cul5-type Ubiquitin Ligase KLHDC1 Contributes to the Elimination of Truncated SELENOS Produced by Failed UGA/Sec Decoding.iScience · 2020Article
- Efficient Generation of Hydrazides in Proteins by RadA Split Intein.Chembiochem : a European journal of chemical biology · 2020Article
- Identification of the Selenoprotein S Positive UGA Recoding (SPUR) element and its position-dependent activity.RNA biology · 2019Article
- Quorum Sensing Regulators AphA and OpaR Control Expression of the Operon Responsible for Biosynthesis of the Compatible Solute Ectoine.Applied and environmental microbiology · 2019Article
- Epitranscriptomic systems regulate the translation of reactive oxygen species detoxifying and disease linked selenoproteins.Free radical biology & medicine · 2019Review
- Differential regulation of cellular stress responses by the endoplasmic reticulum-resident Selenoprotein S (Seps1) in proliferating myoblasts versus myotubes.Physiological reports · 2018Article
- Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis.Cell calcium · 2018Review
- Preparation of Selenocysteine-Containing Forms of Human SELENOK and SELENOS.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Quantification of Membrane Protein-Detergent Complex Interactions.The journal of physical chemistry. B · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Selenoprotein S (SelS or VIMP) is an intrinsically disordered membrane enzyme that provides protection against reactive oxidative species. SelS is a member of the endoplasmic reticulum-associated protein degradation pathway, but its precise enzymatic function is unknown. Because it contains the rare amino acid selenocysteine, it belongs to the family of selenoproteins, which are typically oxidoreductases. Its exact enzymatic function is key to understanding how the cell regulates the response to oxidative stress and thus influences human health and aging. To identify its enzymatic function, we have isolated the selenocysteine-containing enzyme by relying on the aggregation of forms that do not have this reactive residue. That allows us to establish that SelS is primarily a thioredoxin-dependent reductase. It is capable of reducing hydrogen peroxide but is not an efficient or broad-spectrum peroxidase. Only the selenocysteine-containing enzyme is active. In addition, the reduction potential of SelS was determined to be -234 mV using electrospray ionization mass spectrometry. This value is consistent with SelS being a partner of thioredoxin. On the basis of this information, SelS can directly combat reactive oxygen species but is also likely to participate in a signaling pathway, via a yet unidentified substrate.
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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.