Evidence map›Paper›PMID 16431928›Full record

ArticleThe Journal of cell biology2006

In vivo BiFC analysis of Y14 and NXF1 mRNA export complexes: preferential localization within and around SC35 domains.

Ute Schmidt, Karsten Richter, Axel Bernhard Berger, Peter Lichter

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 65 citations in OpenAlex.

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  13. The exon junction complex as a node of post-transcriptional networks.Nature reviews. Molecular cell biology · 2016
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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

4 authors at 1 institution in 1 country.

Ute SchmidtDivision Molecular Genetics, Deutsches Krebsforschungszentrum, D-69120 Heidelberg, Germany.
Karsten Richter
Axel Bernhard Berger
Peter Lichter
German Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bimolecular fluorescence complementation (BiFC) assay, which allows the investigation of interacting molecules in vivo, was applied to study complex formation between the splicing factor Y14 and nuclear export factor 1 (NXF1), which evidence indicates are functionally associated with nuclear mRNA. Y14 linked to the COOH terminus of yellow fluorescent protein (YFP; YC-Y14), and NXF1 fused to the NH2 terminus of YFP (YN-NXF1) expressed in MCF7 cells yielded BiFC upon specific binding. Fluorescence accumulated within and around nuclear speckles, suggesting the involvement of speckles in mRNA processing and export. Accordingly, BiFC depended on transcription and full-length NXF1. Coimmunoprecipitation of YC-Y14 with YN-NXF1, NXF1, Y14, and RNA indicated that YC-Y14 and YN-NXF1 functionally associate with RNA. Fluorescence recovery after photobleaching and fluorescence loss in photobleaching revealed that roughly half of the accumulated BiFC complexes were immobile in vivo. This immobile fraction was readily depleted by adenosine triphosphate (ATP) administration in permeabilized cells. These results suggest that a fraction of RNA, which remains in the nucleus for several hours despite its association with splicing and export proteins, accumulates in speckles because of an ATP-dependent mechanism.

Indexed as

Protein Interaction MappingActive Transport, Cell NucleusAdenosine TriphosphateBacterial ProteinsCell Line, TumorCell Membrane PermeabilityCell NucleusDigitoninFluorescence Recovery After PhotobleachingHumansIntranuclear SpaceKineticsLuminescent ProteinsMutationNuclear ProteinsNucleocytoplasmic Transport ProteinsAdenosine TriphosphateBacterial ProteinsDigitoninLuminescent ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNXF1 protein, humanRBM8A protein, humanRecombinant Fusion ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerRNA Polymerase IISerine-Arginine Splicing FactorsSodium AzideSRSF2 protein, humanyellow fluorescent protein, Bacteria

Identifiers

PMID16431928
PMCPMC2063647
OpenAlexW2019090030

What OpenQuestion holds

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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.