ArticleMolecular and cellular biology2006
Nuclear assembly of UGA decoding complexes on selenoprotein mRNAs: a mechanism for eluding nonsense-mediated decay?
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
- SEPHS1: Its evolution, function and roles in development and diseases.Archives of biochemistry and biophysics · 2022Article
- eIF3 Interacts with Selenoprotein mRNAs.Biomolecules · 2022Article
- Crosstalk between regulated necrosis and micronutrition, bridged by reactive oxygen species.Frontiers in nutrition · 2022Review
- Selenocysteine insertion sequence binding protein 2 (Sbp2) in the sex-specific regulation of selenoprotein gene expression in mouse pancreatic islets.Scientific reports · 2020Article
- Human Disorders Affecting the Selenocysteine Incorporation Pathway Cause Systemic Selenoprotein Deficiency.Antioxidants & redox signaling · 2020Article
- Selenium and selenoproteins: it's role in regulation of inflammation.Inflammopharmacology · 2020Review
- New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.Biological trace element research · 2019Review
- Oxidative Stress Triggers Selective tRNA Retrograde Transport in Human Cells during the Integrated Stress Response.Cell reports · 2019Article
- Article
- Hypermethylated-capped selenoprotein mRNAs in mammals.Nucleic acids research · 2014Article
- Selective up-regulation of human selenoproteins in response to oxidative stress.The Journal of biological chemistry · 2014Article
- Interplay between selenium levels, selenoprotein expression, and replicative senescence in WI-38 human fibroblasts.The Journal of biological chemistry · 2014Article
- Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2.RNA biology · 2014Article
- Threading the needle: getting selenocysteine into proteins.Antioxidants & redox signaling · 2010Review
- Exposure to monomethylarsonous acid (MMA(III)) leads to altered selenoprotein synthesis in a primary human lung cell model.Toxicology and applied pharmacology · 2009Article
- The human selenoproteome: recent insights into functions and regulation.Cellular and molecular life sciences : CMLS · 2009Review
- Regulation and function of selenoproteins in human disease.The Biochemical journal · 2009Review
- Cellular and molecular basis of deiodinase-regulated thyroid hormone signaling.Endocrine reviews · 2008Review
- Functional characterization of alternatively spliced human SECISBP2 transcript variants.Nucleic acids research · 2008Article
- Arsenic trioxide and auranofin inhibit selenoprotein synthesis: implications for chemotherapy for acute promyelocytic leukaemia.British journal of pharmacology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Recoding of UGA from a stop codon to selenocysteine poses a dilemma for the protein translation machinery. In eukaryotes, two factors that are crucial to this recoding process are the mRNA binding protein of the Sec insertion sequence, SBP2, and the specialized elongation factor, EFsec. We sought to determine the subcellular localization of these selenoprotein synthesis factors in mammalian cells and thus gain insight into how selenoprotein mRNAs might circumvent nonsense-mediated decay. Intriguingly, both EFsec and SBP2 localization differed depending on the cell line but significant colocalization of the two proteins was observed in cells where SBP2 levels were detectable. We identify functional nuclear localization and export signals in both proteins, demonstrate that SBP2 undergoes nucleocytoplasmic shuttling, and provide evidence that SBP2 levels and localization may influence EFsec localization. Our results suggest a mechanism for the nuclear assembly of the selenocysteine incorporation machinery that could allow selenoprotein mRNAs to circumvent nonsense-mediated decay, thus providing new insights into the mechanism of selenoprotein translation.
Indexed as
Identifiers
What OpenQuestion holds
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.