Evidence map›Paper›PMID 25277656›Full record

ArticleJournal of molecular biology2014

A highly conserved region essential for NMD in the Upf2 N-terminal domain.

Zaineb Fourati, Bijoyita Roy, Claudia Millan, Pierre-Damien Coureux, Stéphanie Kervestin, Herman van Tilbeurgh, Feng He, Isabel Usón, Allan Jacobson, Marc Graille

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Nonsense-Mediated mRNA Decay Begins Where Translation Ends.Cold Spring Harbor perspectives in biology · 2019
    Review
  8. Review
  9. Review
  10. Article
  11. Mechanism, factors, and physiological role of nonsense-mediated mRNA decay.Cellular and molecular life sciences : CMLS · 2015
    Review
  12. Review
  13. Review
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

10 authors at 4 institutions in 3 countries.

Zaineb FouratiLaboratoire de Biochimie, CNRS UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France; Institut de Biochimie et Biophysique Moléculaire et Cellulaire, CNRS UMR 8619, Université Paris Sud, F-91405 Orsay Cedex, France.
Bijoyita RoyDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Albert Sherman Center, 368 Plantation Street, Worcester, MA 01655-0122, USA.
Claudia MillanInstituto de Biología Molecular de Barcelona, Spanish Research Council, Barcelona Science Park, Baldiri Reixach 15, 08028 Barcelona, Spain; Institució Catalana de Recerca i Estudis Avançats, Passeig Lluís Companys 23, 08010 Barcelona, Spain.
Pierre-Damien CoureuxLaboratoire de Biochimie, CNRS UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France.
Stéphanie KervestinInstitut de Biologie Physico-Chimique, CNRS FRE 3630, Université Paris Diderot Sorbonne Paris Cité, F-75005 Paris, France.
Herman van TilbeurghInstitut de Biochimie et Biophysique Moléculaire et Cellulaire, CNRS UMR 8619, Université Paris Sud, F-91405 Orsay Cedex, France.
Feng HeDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Albert Sherman Center, 368 Plantation Street, Worcester, MA 01655-0122, USA.
Isabel UsónInstituto de Biología Molecular de Barcelona, Spanish Research Council, Barcelona Science Park, Baldiri Reixach 15, 08028 Barcelona, Spain; Institució Catalana de Recerca i Estudis Avançats, Passeig Lluís Companys 23, 08010 Barcelona, Spain.
Allan JacobsonDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Albert Sherman Center, 368 Plantation Street, Worcester, MA 01655-0122, USA. Electronic address: allan.jacobson@umassmed.edu.
Marc GrailleLaboratoire de Biochimie, CNRS UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France; Institut de Biochimie et Biophysique Moléculaire et Cellulaire, CNRS UMR 8619, Université Paris Sud, F-91405 Orsay Cedex, France. Electronic address: marc.graille@polytechnique.edu.
Université Paris-Sud · FRUniversity of Massachusetts Chan Medical School · USCentre National de la Recherche Scientifique · FRInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

Messenger RNA Metabolism in YeastR37GM027757 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JACOBSON, ALLAN S · 2005 to 2014
$6.3M
MESSENGER RNA METABOLISM IN YEASTR01GM027757 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JACOBSON, ALLAN S · 1985 to 2016
$3.8M
NIGMS NIH HHS R01 GM027757NIGMS NIH HHS R37 GM027757NIGMS NIH HHS R37 GM27757
6 · The paper itself

Abstract

Upf1, Upf2, and Upf3 are the principal regulators of nonsense-mediated mRNA decay (NMD), a cytoplasmic surveillance pathway that accelerates the degradation of mRNAs undergoing premature translation termination. These three proteins interact with each other, the ribosome, the translation termination machinery, and multiple mRNA decay factors, but the precise mechanism allowing the selective detection and degradation of nonsense-containing transcripts remains elusive. Here, we have determined the crystal structure of the N-terminal mIF4G domain from Saccharomyces cerevisiae Upf2 and identified a highly conserved region in this domain that is essential for NMD and independent of Upf2's binding sites for Upf1 and Upf3. Mutations within this conserved region not only inactivate NMD but also disrupt Upf2 binding to specific proteins, including Dbp6, a DEAD-box helicase. Although current models indicate that Upf2 functions principally as an activator of Upf1 and a bridge between Upf1 and Upf3, our data suggest that it may also serve as a platform for the association of additional factors that play roles in premature translation termination and NMD.

Indexed as

Adaptor Proteins, Signal TransducingBlotting, NorthernCrystallography, X-RayDEAD-box RNA HelicasesImmunoprecipitationModels, MolecularMutationNonsense Mediated mRNA DecayProtein ConformationProtein Structure, TertiaryRNA-Binding ProteinsRNA HelicasesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAdaptor Proteins, Signal TransducingDEAD-box RNA HelicasesNAM7 protein, S cerevisiaeNMD2 protein, S cerevisiaeRNA-Binding ProteinsRNA HelicasesRNA, MessengerSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsUPF3 protein, S cerevisiaehelicasemIF4G domainsnonsense-mediated mRNA decayRNA binding

Identifiers

PMID25277656
PMCPMC4871600
OpenAlexW2032805036

What OpenQuestion holds

Textmetadata
LicenceTDM
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.