Evidence map›Paper›PMID 26841701›Full record

ArticleNature communications2016

The RNA helicase DHX34 functions as a scaffold for SMG1-mediated UPF1 phosphorylation.

Roberto Melero, Nele Hug, Andrés López-Perrote, Akio Yamashita, Javier F Cáceres, Oscar Llorca

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Nonsense-mediated mRNA decay: friend or foe in cancer biology?Cell communication and signaling : CCS · 2026
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  10. Alternative splicing redefines landscape of commonly mutated genes in acute myeloid leukemia.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

6 authors at 3 institutions in 3 countries.

Roberto MeleroCentro de Investigaciones Biológicas (CIB), Consejo Superior de Investigaciones Científicas (Spanish National Research Council, CSIC), Ramiro de Maeztu 9, Madrid 28040, Spain.
Nele HugMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, Western General Hospital, University of Edinburgh, Edinburgh EH4 2XU, UK.
Andrés López-PerroteCentro de Investigaciones Biológicas (CIB), Consejo Superior de Investigaciones Científicas (Spanish National Research Council, CSIC), Ramiro de Maeztu 9, Madrid 28040, Spain.
Akio YamashitaDepartment of Molecular Biology, Yokohama City University School of Medicine, 3-9, Fukuura, Kanazawa-ku, Yokohama, Kanagawa 236-0004, Japan.
Javier F CáceresMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, Western General Hospital, University of Edinburgh, Edinburgh EH4 2XU, UK.ORCID http://orcid.org/0000-0001-8025-6169
Oscar LlorcaCentro de Investigaciones Biológicas (CIB), Consejo Superior de Investigaciones Científicas (Spanish National Research Council, CSIC), Ramiro de Maeztu 9, Madrid 28040, Spain.
Consejo Superior de Investigaciones Científicas · ESWestern General Hospital · GBYokohama City University · JP

Funding

Medical Research Council MC_PC_U127584479Wellcome Trust 095518/Z/11/Z
6 · The paper itself

Abstract

Nonsense-mediated decay (NMD) is a messenger RNA quality-control pathway triggered by SMG1-mediated phosphorylation of the NMD factor UPF1. In recent times, the RNA helicase DHX34 was found to promote mRNP remodelling, leading to activation of NMD. Here we demonstrate the mechanism by which DHX34 functions in concert with SMG1. DHX34 comprises two distinct structural units, a core that binds UPF1 and a protruding carboxy-terminal domain (CTD) that binds the SMG1 kinase, as shown using truncated forms of DHX34 and electron microscopy of the SMG1-DHX34 complex. Truncation of the DHX34 CTD does not affect binding to UPF1; however, it compromises DHX34 binding to SMG1 to affect UPF1 phosphorylation and hence abrogate NMD. Altogether, these data suggest the existence of a complex comprising SMG1, UPF1 and DHX34, with DHX34 functioning as a scaffold for UPF1 and SMG1. This complex promotes UPF1 phosphorylation leading to functional NMD.

Indexed as

Nonsense Mediated mRNA DecayHEK293 CellsHeLa CellsHumansImmunoprecipitationIn Vitro TechniquesMicroscopy, ElectronPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingProtein Serine-Threonine KinasesRNA HelicasesTrans-ActivatorsDHX34 protein, humanPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesRNA HelicasesSMG1 protein, humanTrans-ActivatorsUPF1 protein, human

Identifiers

PMID26841701
PMCPMC4743010
OpenAlexW2252585587

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.