Evidence map›Paper›PMID 24658146›Full record

ArticlePloS one2014

Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin.

Mohamed S Taha, Kazem Nouri, Lech G Milroy, Jens M Moll, Christian Herrmann, Luc Brunsveld, Roland P Piekorz, Mohammad R Ahmadian

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 66 citations in OpenAlex.

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  6. Review
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  11. The fragile X proteins' enigma: to be or not to be nucleolar.Frontiers in cell and developmental biology · 2024
    Article
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  18. HeterozygousGenes · 2021
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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

8 authors at 3 institutions in 2 countries.

Mohamed S TahaInstitute of Biochemistry and Molecular Biology II, Medical Faculty of the Heinrich-Heine-University, Düsseldorf, Germany.
Kazem NouriInstitute of Biochemistry and Molecular Biology II, Medical Faculty of the Heinrich-Heine-University, Düsseldorf, Germany.
Lech G MilroyLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Technische Universiteit Eindhoven, Eindhoven, the Netherlands.
Jens M MollInstitute of Biochemistry and Molecular Biology II, Medical Faculty of the Heinrich-Heine-University, Düsseldorf, Germany.
Christian HerrmannDepartment of Physical Chemistry I, Ruhr University Bochum, Bochum, Germany.
Luc BrunsveldLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Technische Universiteit Eindhoven, Eindhoven, the Netherlands.
Roland P PiekorzInstitute of Biochemistry and Molecular Biology II, Medical Faculty of the Heinrich-Heine-University, Düsseldorf, Germany.
Mohammad R AhmadianInstitute of Biochemistry and Molecular Biology II, Medical Faculty of the Heinrich-Heine-University, Düsseldorf, Germany.
Heinrich Heine University Düsseldorf · DEEindhoven University of Technology · NLRuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fragile X mental Retardation Protein (FMRP) is a well-known regulator of local translation of its mRNA targets in neurons. However, despite its ubiquitous expression, the role of FMRP remains ill-defined in other cell types. In this study we investigated the subcellular distribution of FMRP and its protein complexes in HeLa cells using confocal imaging as well as detergent-free fractionation and size exclusion protocols. We found FMRP localized exclusively to solid compartments, including cytosolic heavy and light membranes, mitochondria, nuclear membrane and nucleoli. Interestingly, FMRP was associated with nucleolin in both a high molecular weight ribosomal and translation-associated complex (≥6 MDa) in the cytosol, and a low molecular weight complex (∼200 kDa) in the nucleoli. Consistently, we identified two functional nucleolar localization signals (NoLSs) in FMRP that are responsible for a strong nucleolar colocalization of the C-terminus of FMRP with nucleolin, and a direct interaction of the N-terminus of FMRP with the arginine-glycine-glycine (RGG) domain of nucleolin. Taken together, we propose a novel mechanism by which a transient nucleolar localization of FMRP underlies a strong nucleocytoplasmic translocation, most likely in a complex with nucleolin and possibly ribosomes, in order to regulate translation of its target mRNAs.

Indexed as

Cell FractionationFragile X Messenger Ribonucleoprotein 1Gene Expression RegulationHeLa CellsHumansNuclear Localization SignalsNucleolinPhosphoproteinsProtein TransportRNA-Binding ProteinsRNA, MessengerFragile X Messenger Ribonucleoprotein 1Nuclear Localization SignalsNucleolinPhosphoproteinsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID24658146
PMCPMC3962360
OpenAlexW2012855206

What OpenQuestion holds

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LicenceCC BY
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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.