ArticleNucleic acids research2010
Nucleolin binds to a subset of selenoprotein mRNAs and regulates their expression.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 75 citations in OpenAlex.
- Nucleolin Alterations and ROS Production Associate With Sensitivity of AML Cells to Venetoclax.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Genetics of selenoproteins and selenoprotein metabolism - An overview of current concepts and emerging aspects.Redox biology · 2026Review
- Role of Selenium-Dependent Glutathione Peroxidases (Seleno-GPxs) in Radio-Modulation: Lessons for Radiation Oncology.Biological trace element research · 2026Review
- Exploring structural determinants and the role of nucleolin in formation of the long-range interactions between untranslated regions of p53 mRNA.RNA (New York, N.Y.) · 2023Article
- eIF3 Interacts with Selenoprotein mRNAs.Biomolecules · 2022Article
- The Effects of Selenium on Bone Health: From Element to Therapeutics.Molecules (Basel, Switzerland) · 2022Review
- Selenium Metabolism and Biosynthesis of Selenoproteins in the Human Body.Biochemistry. Biokhimiia · 2022Review
- Ribosome Fate during Decoding of UGA-Sec Codons.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
- Cancer Stem Cells and Nucleolin as Drivers of Carcinogenesis.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Identification of the Selenoprotein S Positive UGA Recoding (SPUR) element and its position-dependent activity.RNA biology · 2019Article
- 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
- Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme.Antioxidants (Basel, Switzerland) · 2019Review
- Processive incorporation of multiple selenocysteine residues is driven by a novel feature of the selenocysteine insertion sequence.The Journal of biological chemistry · 2018Article
- The Selenium Transport Protein, Selenoprotein P, Requires Coding Sequence Determinants to Promote Efficient Selenocysteine Incorporation.Journal of molecular biology · 2018Article
- A DNA nanorobot functions as a cancer therapeutic in response to a molecular trigger in vivo.Nature biotechnology · 2018Article
- Multiple RNA structures affect translation initiation and UGA redefinition efficiency during synthesis of selenoprotein P.Nucleic acids research · 2017Article
- SECIS-binding protein 2 interacts with the SMN complex and the methylosome for selenoprotein mRNP assembly and translation.Nucleic acids research · 2017Article
- The RNA-binding protein Secisbp2 differentially modulates UGA codon reassignment and RNA decay.Nucleic acids research · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Selenium, an essential trace element, is incorporated into selenoproteins as selenocysteine (Sec), the 21st amino acid. In order to synthesize selenoproteins, a translational reprogramming event must occur since Sec is encoded by the UGA stop codon. In mammals, the recoding of UGA as Sec depends on the selenocysteine insertion sequence (SECIS) element, a stem-loop structure in the 3' untranslated region of the transcript. The SECIS acts as a platform for RNA-binding proteins, which mediate or regulate the recoding mechanism. Using UV crosslinking, we identified a 110 kDa protein, which binds with high affinity to SECIS elements from a subset of selenoprotein mRNAs. The crosslinking activity was purified by RNA affinity chromatography and identified as nucleolin by mass spectrometry analysis. In vitro binding assays showed that purified nucleolin discriminates among SECIS elements in the absence of other factors. Based on siRNA experiments, nucleolin is required for the optimal expression of certain selenoproteins. There was a good correlation between the affinity of nucleolin for a SECIS and its effect on selenoprotein expression. As selenoprotein transcript levels and localization did not change in siRNA-treated cells, our results suggest that nucleolin selectively enhances the expression of a subset of selenoproteins at the translational level.
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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.