Evidence map›Paper›PMID 28193846›Full record

ArticleMolecular and cellular biology2017

Protein 4.1R Exon 16 3' Splice Site Activation Requires Coordination among TIA1, Pcbp1, and RBM39 during Terminal Erythropoiesis.

Shu-Ching Huang, Henry S Zhang, Brian Yu, Ellen McMahon, Dan T Nguyen, Faye H Yu, Alexander C Ou, Jennie Park Ou, Edward J Benz

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

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  8. Post-transcriptional regulation of erythropoiesis.Blood science (Baltimore, Md.) · 2023
    Review
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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

9 authors at 2 institutions in 1 country.

Shu-Ching HuangDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA shu-ching_huang@dfci.harvard.edu.
Henry S ZhangDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Brian YuDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Ellen McMahonDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Dan T NguyenDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Faye H YuDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Alexander C OuDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Jennie Park OuDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Edward J BenzDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Dana-Farber Cancer Institute · USBrigham and Women's Hospital · US

Funding

THALASSEMIC GLOBIN GENE EXPRESSION IN HUMAN RED CELLSR01HL024385 · NHLBI · YALE UNIVERSITY · PI BENZ, EDWARD J · 1985 to 2011
$3.6M
NHLBI NIH HHS R01 HL024385
6 · The paper itself

Abstract

Exon 16 of protein 4.1R encodes a spectrin/actin-binding peptide critical for erythrocyte membrane stability. Its expression during erythroid differentiation is regulated by alternative pre-mRNA splicing. A UUUUCCCCCC motif situated between the branch point and the 3' splice site is crucial for inclusion. We show that the UUUU region and the last three C residues in this motif are necessary for the binding of splicing factors TIA1 and Pcbp1 and that these proteins appear to act in a collaborative manner to enhance exon 16 inclusion. This element also activates an internal exon when placed in a corresponding intronic position in a heterologous reporter. The impact of these two factors is further enhanced by high levels of RBM39, whose expression rises during erythroid differentiation as exon 16 inclusion increases. TIA1 and Pcbp1 associate in a complex containing RBM39, which interacts with U2AF65 and SF3b155 and promotes U2 snRNP recruitment to the branch point. Our results provide a mechanism for exon 16 3' splice site activation in which a coordinated effort among TIA1, Pcbp1, and RBM39 stabilizes or increases U2 snRNP recruitment, enhances spliceosome A complex formation, and facilitates exon definition through RBM39-mediated splicing regulation.

Indexed as

Alternative SplicingAnimalsBinding SitesCell Line, TumorCytoskeletal ProteinsDNA-Binding ProteinsErythropoiesisHEK293 CellsHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansMembrane ProteinsMiceNuclear ProteinsPhosphoproteinsPoly(A)-Binding ProteinsCytoskeletal ProteinsDNA-Binding Proteinserythrocyte membrane band 4.1 proteinHCC1 autoantigenHeterogeneous-Nuclear RibonucleoproteinsMembrane ProteinsNuclear ProteinsPCBP1 protein, humanPhosphoproteinsPoly(A)-Binding ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSF3B1 protein, humanSplicing Factor U2AFT-Cell Intracellular Antigen-1TIA1 protein, humanU2AF2 protein, humanalternative splicingerythropoiesisPcbp1protein 4.1RRBM39TIA1

Identifiers

PMID28193846
PMCPMC5394280
OpenAlexW2588002753

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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.