Evidence map›Paper›PMID 29429924›Full record

ArticleMolecular cell2018

The TIA1 RNA-Binding Protein Family Regulates EIF2AK2-Mediated Stress Response and Cell Cycle Progression.

Cindy Meyer, Aitor Garzia, Michael Mazzola, Stefanie Gerstberger, Henrik Molina, Thomas Tuschl

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
5.4field-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

81 citing papers in PubMed, 144 citations in OpenAlex.

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  7. RNA-binding proteins connect Exon usage to the chromatin.NAR genomics and bioinformatics · 2025
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21 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Cindy MeyerHoward Hughes Medical Institute and Laboratory for RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, Box 186, New York, NY 10065, USA.
Aitor GarziaHoward Hughes Medical Institute and Laboratory for RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, Box 186, New York, NY 10065, USA.
Michael MazzolaHoward Hughes Medical Institute and Laboratory for RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, Box 186, New York, NY 10065, USA.
Stefanie GerstbergerHoward Hughes Medical Institute and Laboratory for RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, Box 186, New York, NY 10065, USA.
Henrik MolinaProteomics Resource Center, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Thomas TuschlHoward Hughes Medical Institute and Laboratory for RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, Box 186, New York, NY 10065, USA. Electronic address: ttuschl@rockefeller.edu.
Howard Hughes Medical Institute · USRockefeller University · US

Funding

Posttranscriptional regulation by mRNA-binding shuttling and transport proteinsR01GM104962 · NIGMS · ROCKEFELLER UNIVERSITY · PI OHLER, UWE, PATEL, DINSHAW J · 2012 to 2016
$4.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM104962
6 · The paper itself

Abstract

TIA1 and TIAL1 encode a family of U-rich element mRNA-binding proteins ubiquitously expressed and conserved in metazoans. Using PAR-CLIP, we determined that both proteins bind target sites with identical specificity in 3' UTRs and introns proximal to 5' as well as 3' splice sites. Double knockout (DKO) of TIA1 and TIAL1 increased target mRNA abundance proportional to the number of binding sites and also caused accumulation of aberrantly spliced mRNAs, most of which are subject to nonsense-mediated decay. Loss of PRKRA by mis-splicing triggered the activation of the double-stranded RNA (dsRNA)-activated protein kinase EIF2AK2/PKR and stress granule formation. Ectopic expression of PRKRA cDNA or knockout of EIF2AK2 in DKO cells rescued this phenotype. Perturbation of maturation and/or stability of additional targets further compromised cell cycle progression. Our study reveals the essential contributions of the TIA1 protein family to the fidelity of mRNA maturation, translation, and RNA-stress-sensing pathways in human cells.

Indexed as

Cell CycleStress, PhysiologicalCRISPR-Cas SystemsCytoplasmic GranuleseIF-2 KinaseHEK293 CellsHumansRegulatory Sequences, Ribonucleic AcidRNA-Binding ProteinsRNA, Double-StrandedRNA, MessengerRNA Splice SitesRNA SplicingT-Cell Intracellular Antigen-1UridineEIF2AK2 protein, humaneIF-2 KinasePRKRA protein, humanRegulatory Sequences, Ribonucleic AcidRNA-Binding ProteinsRNA, Double-StrandedRNA, MessengerRNA Splice SitesT-Cell Intracellular Antigen-1TIA1 protein, humanTIAL1 protein, humanUridinealternative splicingapoptosiscell cycleeukaryotic translation initiation factor 2 alpha kinase 2integrated stress responseinterferon-inducible double-stranded RNA-dependent protein kinase activator AT-cell restricted intracellular antigen-1

Identifiers

PMID29429924
PMCPMC5816707
OpenAlexW2787167935

What OpenQuestion holds

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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.