Evidence map›Paper›PMID 25921069›Full record

ArticleMolecular cell2015

Global Promotion of Alternative Internal Exon Usage by mRNA 3' End Formation Factors.

Ashish Misra, Jianhong Ou, Lihua J Zhu, Michael R Green

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  4. Coupling of alternative splicing and alternative polyadenylation.Acta biochimica et biophysica Sinica · 2024
    Review
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  18. Influenza virus infection causes global RNAPII termination defects.Nature structural & molecular biology · 2018
    Article
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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.

Ashish MisraHoward Hughes Medical Institute, University of Massachusetts Medical School, Worcester, MA 01605, USA; Department of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Jianhong OuDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Lihua J ZhuDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA; Program in Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Michael R GreenHoward Hughes Medical Institute, University of Massachusetts Medical School, Worcester, MA 01605, USA; Department of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: michael.green@umassmed.edu.
University of Massachusetts Chan Medical School · US

Funding

SPLICING OF MRNA PRECURSORSR01GM035490 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GREEN, MICHAEL R · 1985 to 2021
$4.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM035490NIGMS NIH HHS R01GM035490
6 · The paper itself

Abstract

The mechanisms that regulate alternative precursor mRNA (pre-mRNA) splicing are largely unknown. Here, we perform an RNAi screen to identify factors required for alternative splicing regulation by RBFOX2, an RNA-binding protein that promotes either exon inclusion or exclusion. Unexpectedly, we find that two mRNA 3' end formation factors, cleavage and polyadenylation specificity factor (CPSF) and SYMPK, are RBFOX2 cofactors for both inclusion and exclusion of internal exons. RBFOX2 interacts with CPSF/SYMPK and recruits it to the pre-mRNA. RBFOX2 and CPSF/SYMPK then function together to regulate binding of the early intron recognition factors U2AF and U1 small nuclear ribonucleoprotein particle (snRNP). Genome-wide analysis reveals that CPSF also mediates alternative splicing of many internal exons in the absence of RBFOX2. Accordingly, we show that CPSF/SYMPK is also a cofactor of NOVA2 and heterologous nuclear ribonucleoprotein A1 (HNRNPA1), RNA-binding proteins that also regulate alternative splicing. Collectively, our results reveal an unanticipated role for mRNA 3' end formation factors in global promotion of alternative splicing.

Indexed as

Alternative SplicingBase SequenceCleavage And Polyadenylation Specificity FactorExonsGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHumansNuclear ProteinsProtein BindingRepressor ProteinsRibonucleoproteinsRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA, MessengerRNA Splice SitesCleavage And Polyadenylation Specificity FactorGreen Fluorescent ProteinsNuclear ProteinsRBFOX2 protein, humanRepressor ProteinsRibonucleoproteinsRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA, MessengerRNA Splice SitesRNA Splicing FactorsSplicing Factor U2AFSYMPK protein, humanU2AF2 protein, human

Identifiers

PMID25921069
PMCPMC4458236
OpenAlexW2013810852

What OpenQuestion holds

Textmetadata
LicenceTDM
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.