Evidence map›Paper›PMID 22184459›Full record

ArticleRNA (New York, N.Y.)2012

Mechanisms of activation and repression by the alternative splicing factors RBFOX1/2.

Shuying Sun, Zuo Zhang, Oliver Fregoso, Adrian R Krainer

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 9% 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

78 citing papers in PubMed, 1 synthesis or guideline pooled it, 103 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Science advances · 2025
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  15. Decoding RNA Metabolism by RNA-linked CRISPR Screening in Human Cells.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

18 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

4 authors at 1 institution in 1 country.

Shuying SunCold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
Zuo Zhang
Oliver Fregoso
Adrian R Krainer
Cold Spring Harbor Laboratory · US

Funding

BIOCHEMISTRY OF PREMRNA SPLICINGR01GM042699 · NIGMS · COLD SPRING HARBOR LABORATORY · PI Adrian R Krainer · 1989 to 2026
$8.8M
Biochemistry of Pre-mRNA SplicingR37GM042699 · NIGMS · COLD SPRING HARBOR LABORATORY · PI KRAINER, ADRIAN R · 2012 to 2021
$7.7M
NIGMS NIH HHS GM42699NIGMS NIH HHS R01 GM042699NIGMS NIH HHS R37 GM042699
6 · The paper itself

Abstract

RBFOX1 and RBFOX2 are alternative splicing factors that are predominantly expressed in the brain and skeletal muscle. They specifically bind the RNA element UGCAUG, and regulate alternative splicing positively or negatively in a position-dependent manner. The molecular basis for the position dependence of these and other splicing factors on alternative splicing of their targets is not known. We explored the mechanisms of RBFOX splicing activation and repression using an MS2-tethering assay. We found that the Ala/Tyr/Gly-rich C-terminal domain is sufficient for exon activation when tethered to the downstream intron, whereas both the C-terminal domain and the central RRM are required for exon repression when tethered to the upstream intron. Using immunoprecipitation and mass spectrometry, we identified hnRNP H1, RALY, and TFG as proteins that specifically interact with the C-terminal domain of RBFOX1 and RBFOX2. RNA interference experiments showed that hnRNP H1 and TFG modulate the splicing activity of RBFOX1/2, whereas RALY had no effect. However, TFG is localized in the cytoplasm, and likely modulates alternative splicing indirectly.

Indexed as

Alternative SplicingBinding SitesCell Line, TumorCell NucleusCytoplasmExonsHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear Ribonucleoprotein Group F-HHumansIntronsMutationProtein Interaction Domains and MotifsProteinsProtein Structure, TertiaryRepressor ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear Ribonucleoprotein Group F-HHNRNPH2 protein, humanProteinsRALY protein, humanRBFOX1 protein, humanRBFOX2 protein, humanRepressor ProteinsRNA-Binding ProteinsRNA Splicing FactorsTFG protein, humanVesicular Transport Proteins

Identifiers

PMID22184459
PMCPMC3264914
OpenAlexW2166900174

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.