Evidence map›Paper›PMID 25874565›Full record

ArticlePloS one2015

Age-related nuclear translocation of P2X6 subunit modifies splicing activity interacting with splicing factor 3A1.

Juan Ignacio Díaz-Hernández, Álvaro Sebastián-Serrano, Rosa Gómez-Villafuertes, Miguel Díaz-Hernández, María Teresa Miras-Portugal

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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  7. Article
  8. Intracellular expression of purinoceptors.Purinergic signalling · 2015
    Article
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

5 authors at 2 institutions in 1 country.

Juan Ignacio Díaz-HernándezDepartment of Biochemistry and Molecular Biology, Veterinary School, Complutense University of Madrid, Madrid, Spain; Instituto de Investigación Sanitaria del Hospital Clínico San Carlos, IdISSC, Madrid, Spain.
Álvaro Sebastián-SerranoDepartment of Biochemistry and Molecular Biology, Veterinary School, Complutense University of Madrid, Madrid, Spain; Instituto de Investigación Sanitaria del Hospital Clínico San Carlos, IdISSC, Madrid, Spain.
Rosa Gómez-VillafuertesDepartment of Biochemistry and Molecular Biology, Veterinary School, Complutense University of Madrid, Madrid, Spain; Instituto de Investigación Sanitaria del Hospital Clínico San Carlos, IdISSC, Madrid, Spain.
Miguel Díaz-HernándezDepartment of Biochemistry and Molecular Biology, Veterinary School, Complutense University of Madrid, Madrid, Spain; Instituto de Investigación Sanitaria del Hospital Clínico San Carlos, IdISSC, Madrid, Spain.
María Teresa Miras-PortugalDepartment of Biochemistry and Molecular Biology, Veterinary School, Complutense University of Madrid, Madrid, Spain; Instituto de Investigación Sanitaria del Hospital Clínico San Carlos, IdISSC, Madrid, Spain.
Instituto de Investigación Sanitaria del Hospital Clínico San Carlos · ESUniversidad Complutense de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2X receptors are ligand-gated ion channels sensitive to extracellular nucleotides formed by the assembling of three equal or different P2X subunits. In this work we report, for the first time, the accumulation of the P2X6 subunit inside the nucleus of hippocampal neurons in an age-dependent way. This location is favored by its anchorage to endoplasmic reticulum through its N-terminal domain. The extracellular domain of P2X6 subunit is the key to reach the nucleus, where it presents a speckled distribution pattern and is retained by interaction with the nuclear envelope protein spectrin α2. The in vivo results showed that, once inside the nucleus, P2X6 subunit interacts with the splicing factor 3A1, which ultimately results in a reduction of the mRNA splicing activity. Our data provide new insights into post-transcriptional regulation of mRNA splicing, describing a novel mechanism that could explain why this process is sensitive to changes that occur with age.

Indexed as

Active Transport, Cell NucleusAgingAlternative SplicingAnimalsCell Line, TumorCell NucleusCytosolHippocampusMass SpectrometryMiceMice, Inbred C57BLModels, AnimalNeuronsNuclear EnvelopeReceptors, Purinergic P2Ribonucleoprotein, U2 Small Nuclearpurinoceptor P2X6Receptors, Purinergic P2Ribonucleoprotein, U2 Small Nuclearsplicing factor 3a

Identifiers

PMID25874565
PMCPMC4395284
OpenAlexW2233442504

What OpenQuestion holds

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LicenceCC BY
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.