ArticleThe Journal of biological chemistry2016
A Point Mutation in the Exon Junction Complex Factor Y14 Disrupts Its Function in mRNA Cap Binding and Translation Enhancement.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- An interaction between eIF4A3 and eIF3g drives the internal initiation of translation.Nucleic acids research · 2023Article
- Co-phase separation of Y14 and RNA in vitro and its implication for DNA repair.RNA (New York, N.Y.) · 2023Article
- LncRNA HOTAIRM1 functions in DNA double-strand break repair via its association with DNA repair and mRNA surveillance factors.Nucleic acids research · 2023Article
- Promoter-proximal pausing mediated by the exon junction complex regulates splicing.Nature communications · 2019Article
- Exon junction complex components Y14 and Mago still play a role in budding yeast.Scientific reports · 2019Article
- Expression and gene regulation network ofAging · 2019Article
- Exon junction complex (EJC) core genes play multiple developmental roles in Physalis floridana.Plant molecular biology · 2018Article
- The Interplay between the RNA Decay and Translation Machinery in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Y14 governs p53 expression and modulates DNA damage sensitivity.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic mRNA biogenesis involves a series of interconnected steps mediated by RNA-binding proteins. The exon junction complex core protein Y14 is required for nonsense-mediated mRNA decay (NMD) and promotes translation. Moreover, Y14 binds the cap structure of mRNAs and inhibits the activity of the decapping enzyme Dcp2. In this report, we show that an evolutionarily conserved tryptophan residue (Trp-73) of Y14 is critical for its binding to the mRNA cap structure. A Trp-73 mutant (W73V) bound weakly to mRNAs and failed to protect them from degradation. However, this mutant could still interact with the NMD and mRNA degradation factors and retained partial NMD activity. In addition, we found that the W73V mutant could not interact with translation initiation factors. Overexpression of W73V suppressed reporter mRNA translation in vitro and in vivo and reduced the level of a set of nascent proteins. These results reveal a residue of Y14 that confers cap-binding activity and is essential for Y14-mediated enhancement of translation. Finally, we demonstrated that Y14 may selectively and differentially modulate protein biosynthesis.
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