Evidence map›Paper›PMID 10769024›Full record

ArticleThe Journal of cell biology2000

The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation.

W van der Houven van Oordt, M T Diaz-Meco, J Lozano, A R Krainer, J Moscat, J F Cáceres

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

166 citing papers in PubMed, 361 citations in OpenAlex.

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  18. Protein Kinase C Theta Modulates PCMT1 through hnRNPL to Regulate FOXP3 Stability in Regulatory T Cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2020
    Article
  19. The SF3b complex: splicing and beyond.Cellular and molecular life sciences : CMLS · 2020
    Review
  20. Review

106 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 3 institutions in 3 countries.

W van der Houven van OordtMRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, Scotland, United Kingdom.
M T Diaz-Meco
J Lozano
A R Krainer
J Moscat
J F Cáceres
Centro de Biología Molecular Severo Ochoa · ESWestern General Hospital · GBCold Spring Harbor Laboratory · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
Medical Research Council MC_U127584479NCI NIH HHS CA13106NCI NIH HHS P01 CA013106Wellcome Trust
6 · The paper itself

Abstract

Individual members of the serine-arginine (SR) and heterogeneous nuclear ribonucleoprotein (hnRNP) A/B families of proteins have antagonistic effects in regulating alternative splicing. Although hnRNP A1 accumulates predominantly in the nucleus, it shuttles continuously between the nucleus and the cytoplasm. Some but not all SR proteins also undergo nucleo-cytoplasmic shuttling, which is affected by phosphorylation of their serine/arginine (RS)-rich domain. The signaling mechanisms that control the subcellular localization of these proteins are unknown. We show that exposure of NIH-3T3 and SV-40 transformed green monkey kidney (COS) cells to stress stimuli such as osmotic shock or UVC irradiation, but not to mitogenic activators such as PDGF or EGF, results in a marked cytoplasmic accumulation of hnRNP A1, concomitant with an increase in its phosphorylation. These effects are mediated by the MKK(3/6)-p38 pathway, and moreover, p38 activation is necessary and sufficient for the induction of hnRNP A1 cytoplasmic accumulation. The stress-induced increase in the cytoplasmic levels of hnRNP A/B proteins and the concomitant decrease in their nuclear abundance are paralleled by changes in the alternative splicing pattern of an adenovirus E1A pre-mRNA splicing reporter. These results suggest the intriguing possibility that signaling mechanisms regulate pre-mRNA splicing in vivo by influencing the subcellular distribution of splicing factors.

Indexed as

Alternative SplicingGene Expression RegulationHeterogeneous-Nuclear Ribonucleoprotein Group A-B3T3 CellsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell Line, TransformedCOS CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear RibonucleoproteinsMAP Kinase Kinase 3MAP Kinase Kinase 6MiceMitogen-Activated Protein Kinase KinasesOsmolar ConcentrationPhosphorylationCalcium-Calmodulin-Dependent Protein KinasesHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMap2k3 protein, mouseMap2k6 protein, mouseMAP Kinase Kinase 3MAP Kinase Kinase 6Mitogen-Activated Protein Kinase KinasesProtein-Tyrosine KinasesRecombinant ProteinsRibonucleoproteinsRNA-Binding Proteins

Identifiers

PMID10769024
PMCPMC2175157
OpenAlexW2133841696

What OpenQuestion holds

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LicenceCC BY-NC-SA
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Registered trials

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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.