Evidence map›Paper›PMID 30767021›Full record

ArticleNucleic acids research2019

SAM68 interaction with U1A modulates U1 snRNP recruitment and regulates mTor pre-mRNA splicing.

Suryasree Subramania, Laurence M Gagné, Sébastien Campagne, Victoire Fort, Julia O'Sullivan, Karel Mocaer, Miki Feldmüller, Jean-Yves Masson, Frédéric H T Allain, Samer M Hussein and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-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

17 citing papers in PubMed, 25 citations in OpenAlex.

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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

11 authors at 2 institutions in 2 countries.

Suryasree SubramaniaCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Laurence M GagnéCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Sébastien CampagneInstitute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland.
Victoire FortCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Julia O'SullivanCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Karel MocaerCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Miki FeldmüllerInstitute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland.
Jean-Yves MassonCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Frédéric H T AllainInstitute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland.
Samer M HusseinCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Marc-Étienne HuotCentre de recherche du CHU de Québec-Université Laval (axe Oncologie), Québec, QC G1R 3S3, Canada.
Université Laval · CAETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Src associated in mitosis (SAM68) plays major roles in regulating RNA processing events, such as alternative splicing and mRNA translation, implicated in several developmental processes. It was previously shown that SAM68 regulates the alternative splicing of the mechanistic target of rapamycin (mTor), but the mechanism regulating this process remains elusive. Here, we report that SAM68 interacts with U1 small nuclear ribonucleoprotein (U1 snRNP) to promote splicing at the 5' splice site in intron 5 of mTor. We also show that this direct interaction is mediated through U1A, a core-component of U1snRNP. SAM68 was found to bind the RRM1 domain of U1A through its C-terminal tyrosine rich region (YY domain). Deletion of the U1A-SAM68 interaction domain or mutation in SAM68-binding sites in intron 5 of mTor abrogates U1A recruitment and 5' splice site recognition by the U1 snRNP, leading to premature intron 5 termination and polyadenylation. Taken together, our results provide the first mechanistic study by which SAM68 modulates alternative splicing decision, by affecting U1 snRNP recruitment at 5' splice sites.

Indexed as

RNA SplicingAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBacterial ProteinsBinding SitesCell LineExonsFibroblastsGene DeletionGenes, ReporterGreen Fluorescent ProteinsHumansIntronsLuminescent ProteinsMiceAdaptor Proteins, Signal TransducingBacterial ProteinsGreen Fluorescent ProteinsKhdrbs1 protein, mouseLuminescent ProteinsmTOR protein, mouseRibonucleoprotein, U1 Small NuclearRNARNA-Binding ProteinsRNA PrecursorsTOR Serine-Threonine KinasesU1A proteinyellow fluorescent protein, Bacteria

Identifiers

PMID30767021
PMCPMC6486544
OpenAlexW2913903170

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.