Evidence map›Paper›PMID 26944680›Full record

ArticleGenes & development2016

SR proteins are NXF1 adaptors that link alternative RNA processing to mRNA export.

Michaela Müller-McNicoll, Valentina Botti, Antonio M de Jesus Domingues, Holger Brandl, Oliver D Schwich, Michaela C Steiner, Tomaz Curk, Ina Poser, Kathi Zarnack, Karla M Neugebauer

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers.

0numbers the graph read from it
0cells of the map it votes in
180citing papers in PubMed
–field-weighted citation impact
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

180 citing papers in PubMed, 328 citations in OpenAlex.

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120 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

10 authors at 6 institutions in 3 countries.

Michaela Müller-McNicollRNA Regulation Group, Institute of Cell Biology and Neuroscience, Goethe-University Frankfurt, 60438 Frankfurt/Main, Germany;
Valentina BottiDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA;
Antonio M de Jesus DominguesInstitute of Molecular Biology (IMB), 55128 Mainz, Germany;
Holger BrandlMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;
Oliver D SchwichRNA Regulation Group, Institute of Cell Biology and Neuroscience, Goethe-University Frankfurt, 60438 Frankfurt/Main, Germany; Buchmann Institute for Life Sciences (BMLS), 60438 Frankfurt/Main, Germany;
Michaela C SteinerMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;
Tomaz CurkFaculty of Computer and Information Science, University of Ljubljana, Ljubljana 1000, Slovenia.
Ina PoserMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;
Kathi ZarnackBuchmann Institute for Life Sciences (BMLS), 60438 Frankfurt/Main, Germany;
Karla M NeugebauerDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA;
Max Planck Institute of Molecular Cell Biology and Genetics · DEGoethe University Frankfurt · DEYale University · USBeilstein-Institut · DEInstitute of Molecular Biology · DEUniversity of Ljubljana · SI

Funding

Yale Pathology Tissue Services Shared ResourceP30CA016359 · NCI · YALE UNIVERSITY · PI DAVID L RIMM · 1985 to 2026
$85.0M
NCI NIH HHS P30 CA016359
6 · The paper itself

Abstract

Nuclear export factor 1 (NXF1) exports mRNA to the cytoplasm after recruitment to mRNA by specific adaptor proteins. How and why cells use numerous different export adaptors is poorly understood. Here we critically evaluate members of the SR protein family (SRSF1-7) for their potential to act as NXF1 adaptors that couple pre-mRNA processing to mRNA export. Consistent with this proposal, >1000 endogenous mRNAs required individual SR proteins for nuclear export in vivo. To address the mechanism, transcriptome-wide RNA-binding profiles of NXF1 and SRSF1-7 were determined in parallel by individual-nucleotide-resolution UV cross-linking and immunoprecipitation (iCLIP). Quantitative comparisons of RNA-binding sites showed that NXF1 and SR proteins bind mRNA targets at adjacent sites, indicative of cobinding. SRSF3 emerged as the most potent NXF1 adaptor, conferring sequence specificity to RNA binding by NXF1 in last exons. Interestingly, SRSF3 and SRSF7 were shown to bind different sites in last exons and regulate 3' untranslated region length in an opposing manner. Both SRSF3 and SRSF7 promoted NXF1 recruitment to mRNA. Thus, SRSF3 and SRSF7 couple alternative splicing and polyadenylation to NXF1-mediated mRNA export, thereby controlling the cytoplasmic abundance of transcripts with alternative 3' ends.

Indexed as

3' Untranslated RegionsActive Transport, Cell NucleusAlternative SplicingAnimalsCell LineMiceNuclear ProteinsNucleocytoplasmic Transport ProteinsProtein BindingReproducibility of ResultsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSerine-Arginine Splicing Factors3' Untranslated RegionsNuclear ProteinsNucleocytoplasmic Transport ProteinsNXF1 protein, mouseRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSerine-Arginine Splicing FactorsSRSF2 protein, mousealternative 3′ end processingiCLIPmRNA exportNXF1SR proteinSRSF3SRSF7

Identifiers

PMID26944680
PMCPMC4782049
OpenAlexW2291938858

What OpenQuestion holds

Textmetadata
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.