Evidence map›Paper›PMID 15456888›Full record

ArticleMolecular and cellular biology2004

The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo.

Kai-Ti Lin, Ruei-Min Lu, Woan-Yuh Tarn

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

45 citing papers in PubMed, 92 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

3 authors at 1 institution in 1 country.

Kai-Ti LinInstitute of Biomedical Sciences, Academia Sinica, 128 Academy Rd., Section 2, Nankang, Taipei 11529, Taiwan.
Ruei-Min Lu
Woan-Yuh Tarn
Institute of Biomedical Sciences, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A growing body of evidence supports the coordination of mRNA synthesis and its subsequent processing events. Nuclear proteins harboring both WW and FF protein interaction modules bind to splicing factors as well as RNA polymerase II and may serve to link transcription with splicing. To understand how WW domains coordinate the assembly of splicing complexes, we used glutathione S-transferase fusions containing WW domains from CA150 or FBP11 in pull-down experiments with HeLa cell nuclear extract. The WW domains associate preferentially with the U2 small nuclear ribonucleoprotein and with splicing factors SF1, U2AF, and components of the SF3 complex. Accordingly, WW domain-associating factors bind to the 3' part of a pre-mRNA to form a pre-spliceosome-like complex. We performed both in vitro and in vivo splicing assays to explore the role of WW/FF domain-containing proteins in this process. However, although CA150 is associated with the spliceosome, it appears to be dispensable for splicing in vitro. Nevertheless, in vivo depletion of CA150 substantially reduced splicing efficiency of a reporter pre-mRNA. Moreover, overexpression of CA150 fragments containing both WW and FF domains activated splicing and modulated alternative exon selection, probably by facilitating 3' splice site recognition. Our results suggest an essential role of WW/FF domain-containing factors in pre-mRNA splicing that likely occurs in concert with transcription in vivo.

Indexed as

RNA SplicingAnimalsCarrier ProteinsDNA-Binding ProteinsExonsHeLa CellsHumansMacromolecular SubstancesMiceNuclear ProteinsProtein Structure, TertiaryRecombinant Fusion ProteinsRibonucleoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, MessengerCarrier ProteinsDNA-Binding ProteinsFnbp3 protein, mouseMacromolecular SubstancesNuclear ProteinsRecombinant Fusion ProteinsRibonucleoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, MessengerRNA Polymerase IIRNA PrecursorsRNA Splicing FactorsSF1 protein, humanSplicing Factor U2AFTCERG1 protein, humanTrans-ActivatorsTranscriptional Elongation FactorsTranscription FactorsU2AF2 protein, humanZrsr1 protein, mouse

Identifiers

PMID15456888
PMCPMC517884
OpenAlexW2127522716

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.