Evidence map›Paper›PMID 35451102›Full record

ArticleThe EMBO journal2022

Mammalian UPF3A and UPF3B can activate nonsense-mediated mRNA decay independently of their exon junction complex binding.

Zhongxia Yi, René M Arvola, Sean Myers, Corinne N Dilsavor, Rabab Abu Alhasan, Bayley N Carter, Robert D Patton, Ralf Bundschuh, Guramrit Singh

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  5. Review
  6. Gene regulation through exon junction complex modularity.Nature structural & molecular biology · 2025
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Zhongxia YiCenter for RNA Biology, The Ohio State University, Columbus, OH, USA.ORCID 0000-0002-6360-881X
René M ArvolaCenter for RNA Biology, The Ohio State University, Columbus, OH, USA.ORCID 0000-0002-5778-0496
Sean MyersDepartment of Physics, The Ohio State University, Columbus, OH, USA.
Corinne N DilsavorDepartment of Molecular Genetics, The Ohio State University, Columbus, OH, USA.ORCID 0000-0002-6307-7852
Rabab Abu AlhasanCenter for RNA Biology, The Ohio State University, Columbus, OH, USA.ORCID 0000-0002-2277-7457
Bayley N CarterDepartment of Molecular Genetics, The Ohio State University, Columbus, OH, USA.ORCID 0000-0002-4645-8450
Robert D PattonCenter for RNA Biology, The Ohio State University, Columbus, OH, USA.
Ralf BundschuhCenter for RNA Biology, The Ohio State University, Columbus, OH, USA.
Guramrit SinghCenter for RNA Biology, The Ohio State University, Columbus, OH, USA.ORCID 0000-0002-5283-9540
The Ohio State University · US

Funding

Regulation of RNA surveillance by the dynamic Exon Junction ComplexR01GM120209 · NIGMS · OHIO STATE UNIVERSITY · PI SINGH, GURAMRIT · 2017 to 2021
$1.6M
Typhoon FLA9500 Biomedical ImagerS10OD023582 · OD · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH · 2017 to 2017
$144k
Investigating Casc3 function in localized mRNA regulation and neuromuscular developmentF32NS119378 · NINDS · OHIO STATE UNIVERSITY · PI ARVOLA, RENE MARLENE · 2020 to 2022
$121k
NIGMS NIH HHS R01 GM120209NIH HHS S10 OD023582NINDS NIH HHS F32 NS119378
6 · The paper itself

Abstract

Nonsense-mediated mRNA decay (NMD) is governed by the three conserved factors-UPF1, UPF2, and UPF3. While all three are required for NMD in yeast, UPF3B is dispensable for NMD in mammals, and its paralog UPF3A is suggested to only weakly activate or even repress NMD due to its weaker binding to the exon junction complex (EJC). Here, we characterize the UPF3A/B-dependence of NMD in human cell lines deleted of one or both UPF3 paralogs. We show that in human colorectal cancer HCT116 cells, NMD can operate in a UPF3B-dependent and -independent manner. While UPF3A is almost dispensable for NMD in wild-type cells, it strongly activates NMD in cells lacking UPF3B. Notably, NMD remains partially active in cells lacking both UPF3 paralogs. Complementation studies in these cells show that EJC-binding domain of UPF3 paralogs is dispensable for NMD. Instead, the conserved "mid" domain of UPF3 paralogs is consequential for their NMD activity. Altogether, our results demonstrate that the mammalian UPF3 proteins play a more active role in NMD than simply bridging the EJC and the UPF complex.

Indexed as

Nonsense Mediated mRNA DecayRNA-Binding ProteinsExonsHCT116 CellsHumansRNA HelicasesTrans-ActivatorsRNA-Binding ProteinsRNA HelicasesTrans-ActivatorsUPF3A protein, humanUPF3B protein, humanexon junction complexmRNA degradationnonsense-mediated mRNA decaynonsense mutationstranslation termination

Identifiers

PMID35451102
PMCPMC9108626
OpenAlexW4224265630

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.