ArticlePloS one2012
Selenocysteine insertion sequence binding protein 2L is implicated as a novel post-transcriptional regulator of selenoprotein expression.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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
21 citing papers in PubMed, 30 citations in OpenAlex.
- Genetics of selenoproteins and selenoprotein metabolism - An overview of current concepts and emerging aspects.Redox biology · 2026Review
- Sbp2l contributes to oligodendrocyte maturation through translational control in Tcf7l2 signaling.iScience · 2023Article
- High-Resolution Ribosome Profiling Reveals Gene-Specific Details of UGA Re-Coding in Selenoprotein Biosynthesis.Biomolecules · 2022Article
- Selenocysteine Machinery Primarily Supports TXNRD1 and GPX4 Functions and Together They Are Functionally Linked with SCD and PRDX6.Biomolecules · 2022Article
- SECISBP2L-Mediated Selenoprotein Synthesis Is Essential for Autonomous Regulation of Oligodendrocyte Differentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- The expression of essential selenoproteins during development requires SECIS-binding protein 2-like.Life science alliance · 2022Article
- Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021Review
- Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery.International journal of molecular sciences · 2021Review
- SECISBP2 is a novel prognostic predictor that regulates selenoproteins in diffuse large B-cell lymphoma.Laboratory investigation; a journal of technical methods and pathology · 2021Article
- Tolerance to Selenoprotein Loss Differs between Human and Mouse.Molecular biology and evolution · 2020Article
- Processive Recoding and Metazoan Evolution of Selenoprotein P: Up to 132 UGAs in Molluscs.Journal of molecular biology · 2019Article
- New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.Biological trace element research · 2019Review
- The RNA-binding protein Secisbp2 differentially modulates UGA codon reassignment and RNA decay.Nucleic acids research · 2017Article
- A quantitative model for the rate-limiting process of UGA alternative assignments to stop and selenocysteine codons.PLoS computational biology · 2017Article
- Review
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2.RNA biology · 2014Article
- The molecular biology of selenocysteine.Biomolecular concepts · 2013Review
- Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.Journal of molecular biology · 2013Article
- Alternative transcripts and 3'UTR elements govern the incorporation of selenocysteine into selenoprotein S.PloS one · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The amino acid selenocysteine (Sec) is encoded by UGA codons. Recoding of UGA from stop to Sec requires a Sec insertion sequence (SECIS) element in the 3' UTR of selenoprotein mRNAs. SECIS binding protein 2 (SBP2) binds the SECIS element and is essential for Sec incorporation into the nascent peptide. SBP2-like (SBP2L) is a paralogue of SBP2 in vertebrates and is the only SECIS binding protein in some invertebrates where it likely directs Sec incorporation. However, vertebrate SBP2L does not promote Sec incorporation in in vitro assays. Here we present a comparative analysis of SBP2 and SBP2L SECIS binding properties and demonstrate that its inability to promote Sec incorporation is not due to lower SECIS affinity but likely due to lack of a SECIS dependent domain association that is found in SBP2. Interestingly, however, we find that an invertebrate version of SBP2L is fully competent for Sec incorporation in vitro. Additionally, we present the first evidence that SBP2L interacts with selenoprotein mRNAs in mammalian cells, thereby implying a role in selenoprotein expression.
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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.