Evidence map›Paper›PMID 29244122›Full record

ArticleNucleic acids research2018

La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region.

Lucas Philippe, Jean-Jacques Vasseur, Françoise Debart, Carson C Thoreen

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
5.7field-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

78 citing papers in PubMed, 134 citations in OpenAlex.

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18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Lucas PhilippeDepartment of Cellular and Molecular Physiology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
Jean-Jacques VasseurDepartment of Nucleic Acids, IBMM, Université de Montpellier, CNRS UMR 5247, ENSCM, Montpellier, France.
Françoise DebartDepartment of Nucleic Acids, IBMM, Université de Montpellier, CNRS UMR 5247, ENSCM, Montpellier, France.
Carson C ThoreenDepartment of Cellular and Molecular Physiology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
Yale University · USInstitut des Biomolécules Max Mousseron · FRUniversité de Montpellier · FR

Funding

Translational control of gene expression by the mTOR pathwayR01GM125955 · NIGMS · YALE UNIVERSITY · PI THOREEN, CARSON CORNELL · 2017 to 2021
$1.8M
NIGMS NIH HHS R01 GM125955
6 · The paper itself

Abstract

Cell growth is a complex process shaped by extensive and coordinated changes in gene expression. Among these is the tightly regulated translation of a family of growth-related mRNAs defined by a 5' terminal oligopyrimidine (TOP) motif. TOP mRNA translation is partly controlled via the eukaryotic initiation factor 4F (eIF4F), a translation factor that recognizes the mRNA 5' cap structure. Recent studies have also implicated La-related protein 1 (LARP1), which competes with eIF4F for binding to mRNA 5' ends. However, it has remained controversial whether LARP1 represses TOP mRNA translation directly and, if so, what features define its mRNA targets. Here, we show that the C-terminal half of LARP1 is necessary and sufficient to control TOP mRNA translation in cells. This fragment contains the DM15 cap-binding domain as well as an adjacent regulatory region that we identified. We further demonstrate that purified LARP1 represses TOP mRNA translation in vitro through the combined recognition of both the TOP sequence and cap structure, and that its intrinsic repressive activity and affinity for these features are subject to regulation. These results support a model whereby the translation of TOP mRNAs is controlled by a growth-regulated competition between eIF4F and LARP1 for their 5' ends.

Indexed as

Protein BiosynthesisAutoantigensBase SequenceBinding, CompetitiveBinding SitesCell-Free SystemComputational BiologyEukaryotic Initiation Factor-4FGene Expression RegulationHEK293 CellsHumansMechanistic Target of Rapamycin Complex 1Models, GeneticPolyribosomesProtein BindingProtein Interaction Domains and MotifsAutoantigensEukaryotic Initiation Factor-4FMechanistic Target of Rapamycin Complex 1PyrimidinesRibonucleoproteinsRNA, MessengerSS-B Antigen

Identifiers

PMID29244122
PMCPMC5814973
OpenAlexW2771265500

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.