Evidence map›Paper›PMID 24297750›Full record

ArticleThe Journal of cell biology2013

The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules.

Kyota Yasuda, Huaye Zhang, David Loiselle, Timothy Haystead, Ian G Macara, Stavroula Mili

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
5.5field-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

109 citing papers in PubMed, 177 citations in OpenAlex.

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49 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 5 institutions in 1 country.

Kyota YasudaLaboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
Huaye Zhang
David Loiselle
Timothy Haystead
Ian G Macara
Stavroula Mili
Duke University · USNational Cancer Institute · USNational Institutes of Health · USRutgers, The State University of New Jersey · USVanderbilt University Medical Center · US

Funding

Regulation and functional effects of localized RNAsZIABC011501 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MILI, STAVROULA · 2013 to 2025
$16.3M
MECHANISMS OF CELL POLARITY ESTABLISHMENTR01GM070902 · NIGMS · VANDERBILT UNIVERSITY · PI MACARA, IAN G · 2004 to 2022
$5.4M
The PAR-6/aPKC Polarity Complex in Synaptic Assembly and FunctionR00NS065183 · NINDS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI ZHANG, HUAYE · 2011 to 2013
$738k
RNA localization and tumor suppression by APCK99CA138905 · NCI · UNIVERSITY OF VIRGINIA · PI MILI, STAVROULA · 2009 to 2010
$198k
NCI NIH HHS CA138905NCI NIH HHS K99 CA138905NIGMS NIH HHS R01 GM070902NINDS NIH HHS R00 NS065183
6 · The paper itself

Abstract

RNA localization pathways direct numerous mRNAs to distinct subcellular regions and affect many physiological processes. In one such pathway the tumor-suppressor protein adenomatous polyposis coli (APC) targets RNAs to cell protrusions, forming APC-containing ribonucleoprotein complexes (APC-RNPs). Here, we show that APC-RNPs associate with the RNA-binding protein Fus/TLS (fused in sarcoma/translocated in liposarcoma). Fus is not required for APC-RNP localization but is required for efficient translation of associated transcripts. Labeling of newly synthesized proteins revealed that Fus promotes translation preferentially within protrusions. Mutations in Fus cause amyotrophic lateral sclerosis (ALS) and the mutant protein forms inclusions that appear to correspond to stress granules. We show that overexpression or mutation of Fus results in formation of granules, which preferentially recruit APC-RNPs. Remarkably, these granules are not translationally silent. Instead, APC-RNP transcripts are translated within cytoplasmic Fus granules. These results unexpectedly show that translation can occur within stress-like granules. Importantly, they identify a new local function for cytoplasmic Fus with implications for ALS pathology.

Indexed as

Protein BiosynthesisAdenomatous Polyposis Coli ProteinAnimalsCytoplasmic GranulesMiceNIH 3T3 CellsRibonucleoproteinsRNA-Binding Protein FUSRNA, MessengerAdenomatous Polyposis Coli ProteinRibonucleoproteinsRNA-Binding Protein FUSRNA, Messenger

Identifiers

PMID24297750
PMCPMC3857475
OpenAlexW2068994511

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.