Evidence map›Paper›PMID 26763119›Full record

ArticleRNA (New York, N.Y.)2016

Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements.

Rui Fu, Myanna T Olsen, Kristofor Webb, Eric J Bennett, Jens Lykke-Andersen

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 83 citations in OpenAlex.

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  19. SARS-CoV-2 impairs interferon production via NSP2-induced repression of mRNA translation.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

5 authors at 1 institution in 1 country.

Rui FuDivision of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.
Myanna T OlsenDivision of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.
Kristofor WebbDivision of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.
Eric J BennettDivision of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.
Jens Lykke-AndersenDivision of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.
University of California San Diego · US

Funding

The Function of Processing Bodies in Human mRNA TurnoverR01GM077243 · NIGMS · UNIVERSITY OF COLORADO · PI LYKKE-ANDERSEN, JENS · 2007 to 2015
$1.7M
NIGMS NIH HHS R01 GM077243
6 · The paper itself

Abstract

The zinc finger protein tristetraprolin (TTP) promotes translation repression and degradation of mRNAs containing AU-rich elements (AREs). Although much attention has been directed toward understanding the decay process and machinery involved, the translation repression role of TTP has remained poorly understood. Here we identify the cap-binding translation repression 4EHP-GYF2 complex as a cofactor of TTP. Immunoprecipitation and in vitro pull-down assays demonstrate that TTP associates with the 4EHP-GYF2 complex via direct interaction with GYF2, and mutational analyses show that this interaction occurs via conserved tetraproline motifs of TTP. Mutant TTP with diminished 4EHP-GYF2 binding is impaired in its ability to repress a luciferase reporter ARE-mRNA. 4EHP knockout mouse embryonic fibroblasts (MEFs) display increased induction and slower turnover of TTP-target mRNAs as compared to wild-type MEFs. Our work highlights the function of the conserved tetraproline motifs of TTP and identifies 4EHP-GYF2 as a cofactor in translational repression and mRNA decay by TTP.

Indexed as

AU Rich ElementsAnimalsCell LineEukaryotic Initiation Factor-4EHydrolysisMiceMice, KnockoutProlineProtein BindingRepressor ProteinsRNA CapsRNA, MessengerTristetraprolineIF4E2 protein, mouseEukaryotic Initiation Factor-4EProlineRepressor ProteinsRNA CapsRNA, MessengerTristetraprolinARE-mediated decayAU-rich elementsmRNA turnovertranslation repressiontristetraprolin

Identifiers

PMID26763119
PMCPMC4748815
OpenAlexW2239940604

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.