Evidence map›Paper›PMID 22083953›Full record

ArticleMolecular and cellular biology2012

RBFOX2 promotes protein 4.1R exon 16 selection via U1 snRNP recruitment.

Shu-Ching Huang, Alexander C Ou, Jennie Park, Faye Yu, Brian Yu, Angela Lee, Guang Yang, Anyu Zhou, Edward J Benz

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

  1. Circular RNAs in ferroptosis regulation and tumor progression of gynecological and breast cancers: molecular mechanisms and therapeutic potential.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
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  16. Life and Death of mRNA Molecules inFrontiers in cellular and infection microbiology · 2018
    Review
  17. TheFrontiers in cellular and infection microbiology · 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

9 authors at 4 institutions in 1 country.

Shu-Ching HuangDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA. shu-ching_huang@dfci.harvard.edu
Alexander C Ou
Jennie Park
Faye Yu
Brian Yu
Angela Lee
Guang Yang
Anyu Zhou
Edward J Benz
Harvard University · USDana-Farber Cancer Institute · USBrigham and Women's Hospital · USDana-Farber Brigham Cancer Center · 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 HL24385NHLBI NIH HHS R01 HL024385
6 · The paper itself

Abstract

The erythroid differentiation-specific splicing switch of protein 4.1R exon 16, which encodes a spectrin/actin-binding peptide critical for erythrocyte membrane stability, is modulated by the differentiation-induced splicing factor RBFOX2. We have now characterized the mechanism by which RBFOX2 regulates exon 16 splicing through the downstream intronic element UGCAUG. Exon 16 possesses a weak 5' splice site (GAG/GTTTGT), which when strengthened to a consensus sequence (GAG/GTAAGT) leads to near-total exon 16 inclusion. Impaired RBFOX2 binding reduces exon 16 inclusion in the context of the native weak 5' splice site, but not the engineered strong 5' splice site, implying that RBFOX2 achieves its effect by promoting utilization of the weak 5' splice site. We further demonstrate that RBFOX2 increases U1 snRNP recruitment to the weak 5' splice site through direct interaction between its C-terminal domain (CTD) and the zinc finger region of U1C and that the CTD is required for the effect of RBFOX2 on exon 16 splicing. Our data suggest a novel mechanism for exon 16 5' splice site activation in which the binding of RBFOX2 to downstream intronic splicing enhancers stabilizes the pre-mRNA-U1 snRNP complex through interactions with U1C.

Indexed as

ExonsBase SequenceCytoskeletal ProteinsHEK293 CellsHeLa CellsHumansMembrane ProteinsProtein Structure, TertiaryRepressor ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA SplicingRNA Splicing FactorsZinc FingersCytoskeletal Proteinserythrocyte membrane band 4.1 proteinMembrane ProteinsRBFOX2 protein, humanRepressor ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsRNA Splicing Factors

Identifiers

PMID22083953
PMCPMC3255763
OpenAlexW2161040561

What OpenQuestion holds

Textmetadata
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.