Evidence map›Paper›PMID 15024032›Full record

ArticleThe Journal of cell biology2004

In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160.

Stefan Wagner, Simion Chiosea, Maria Ivshina, Jeffrey A Nickerson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

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  13. Subnuclear localization and intranuclear trafficking of transcription factors.Methods in molecular biology (Clifton, N.J.) · 2010
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  18. Mechanism of mRNA transport in the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2005
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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.

Stefan WagnerDept. of Cell Biology, S7-214, University of Massachusetts Medical School, 55 Lake Ave., Worcester, MA 01655, USA.
Simion Chiosea
Maria Ivshina
Jeffrey A Nickerson
University of Massachusetts Chan Medical School · US

Funding

SUBNUCLEAR TARGETING OF TRANSCRIPTION FACTORSP01CA082834 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, GARY S. · 2001 to 2015
$18.4M
NCI NIH HHS P01 CA082834NCI NIH HHS P01 CA82834
6 · The paper itself

Abstract

We present a new in vitro system for characterizing the binding and mobility of enhanced green fluorescent protein (EGFP)-labeled nuclear proteins by fluorescence recovery after photobleaching in digitonin-permeabilized cells. This assay reveals that SRm160, a splicing coactivator and component of the exon junction complex (EJC) involved in RNA export, has an adenosine triphosphate (ATP)-dependent mobility. Endogenous SRm160, lacking the EGFP moiety, could also be released from sites at splicing speckled domains by an ATP-dependent mechanism. A second EJC protein, RNPS1, also has an ATP-dependent mobility, but SRm300, a protein that binds to SRm160 and participates with it in RNA splicing, remains immobile after ATP supplementation. This finding suggests that SRm160-containing RNA export, but not splicing, complexes have an ATP-dependent mobility. We propose that RNA export complexes have an ATP-regulated mechanism for release from binding sites at splicing speckled domains. In vitro fluorescence recovery after photobleaching is a powerful tool for identifying cofactors required for nuclear binding and mobility.

Indexed as

ExonsActive Transport, Cell NucleusAdenosine TriphosphateAntigens, NuclearCell NucleusFluorescence Recovery After PhotobleachingHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein Group A-BHumansMacromolecular SubstancesNuclear Matrix-Associated ProteinsPermeabilityRecombinant Fusion ProteinsRibonucleoproteinsRNARNA-Binding ProteinsAdenosine TriphosphateAntigens, NuclearHeterogeneous-Nuclear Ribonucleoprotein Group A-BhnRNP A2Macromolecular SubstancesNuclear Matrix-Associated ProteinsRecombinant Fusion ProteinsRibonucleoproteinsRNARNA-Binding ProteinsRNPS1 protein, humanSRRM1 protein, humanSRRM2 protein, human

Identifiers

PMID15024032
PMCPMC2172284
OpenAlexW2136237690

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.