Evidence map›Paper›PMID 22386318›Full record

ArticleCell2012

Coding region polyadenylation generates a truncated tRNA synthetase that counters translation repression.

Peng Yao, Alka A Potdar, Abul Arif, Partho Sarothi Ray, Rupak Mukhopadhyay, Belinda Willard, Yichi Xu, Jun Yan, Gerald M Saidel, Paul L Fox

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing 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

72 citing papers in PubMed, 97 citations in OpenAlex.

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  20. Tryptophanyl-tRNA Synthetase as a Potential Therapeutic Target.International journal of molecular sciences · 2021
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 3 countries.

Peng YaoDepartment of Cell Biology, The Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Alka A Potdar
Abul Arif
Partho Sarothi Ray
Rupak Mukhopadhyay
Belinda Willard
Yichi Xu
Jun Yan
Gerald M Saidel
Paul L Fox
Cleveland Clinic Lerner College of Medicine · USCase Western Reserve University · USChinese Academy of Sciences · CNIndian Institute of Science Education and Research Kolkata · INTezpur University · IN

Funding

Vascular Cell function and AtherosclerosisP01HL029582 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI FOX, PAUL L · 1985 to 2019
$32.0M
Structural Determinants Of Ceruloplasmin Inflammatory ActivityP01HL076491 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 2004 to 2019
$27.3M
A protein-directed RNA switch that regulates translationR01GM086430 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI FOX, PAUL L · 2009 to 2016
$2.6M
Multi-level analysis of iron metabolism and treatment of chronic kidney diseaseR01DK083359 · NIDDK · CLEVELAND CLINIC LERNER COM-CWRU · PI FOX, PAUL L · 2010 to 2013
$2.2M
NHLBI NIH HHS P01 HL029582NHLBI NIH HHS P01 HL076491NIDDK NIH HHS R01 DK083359NIGMS NIH HHS R01 GM086430
6 · The paper itself

Abstract

Posttranscriptional regulatory mechanisms superimpose "fine-tuning" control upon "on-off" switches characteristic of gene transcription. We have exploited computational modeling with experimental validation to resolve an anomalous relationship between mRNA expression and protein synthesis. The GAIT (gamma-interferon-activated inhibitor of translation) complex repressed VEGF-A synthesis to a low, constant rate independent of VEGF-A mRNA expression levels. Dynamic model simulations predicted an inhibitory GAIT-element-interacting factor to account for this relationship and led to the identification of a truncated form of glutamyl-prolyl tRNA synthetase (EPRS), a GAIT constituent that mediates binding to target transcripts. The truncated protein, EPRS(N1), shields GAIT-element-bearing transcripts from the inhibitory GAIT complex, thereby dictating a "translational trickle" of GAIT target proteins. EPRS(N1) mRNA is generated by polyadenylation-directed conversion of a Tyr codon in the EPRS-coding sequence to a stop codon (PAY(∗)). Genome-wide analysis revealed multiple candidate PAY(∗) targets, including the authenticated target RRM1, suggesting a general mechanism for production of C terminus-truncated regulatory proteins.

Indexed as

Gene Expression RegulationGenome, HumanProtein BiosynthesisAmino Acid SequenceAmino Acyl-tRNA SynthetasesCodon, TerminatorHumansLeukocytes, MononuclearMolecular Sequence DataMultiprotein ComplexesPolyadenylationTranscriptomeU937 CellsVascular Endothelial Growth Factor AAmino Acyl-tRNA SynthetasesCodon, Terminatorglutamyl-prolyl-tRNA synthetaseMultiprotein ComplexesVascular Endothelial Growth Factor A

Identifiers

PMID22386318
PMCPMC3615456
OpenAlexW2132040328

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.