Evidence map›Paper›PMID 18573872›Full record

ArticleMolecular and cellular biology2008

Repression of prespliceosome complex formation at two distinct steps by Fox-1/Fox-2 proteins.

Hua-Lin Zhou, Hua Lou

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. Pooled it
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  8. Far upstream element-binding protein 1 and RNA secondary structure both mediate second-step splicing repression.Proceedings of the National Academy of Sciences of the United States of America · 2013
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  18. Fox-1 family of RNA-binding proteins.Cellular and molecular life sciences : CMLS · 2009
    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

2 authors at 1 institution in 1 country.

Hua-Lin ZhouDepartment of Genetics, Case Western Reserve University, 10900 Euclid Ave., Cleveland, OH 44106, USA.
Hua Lou
Case Western Reserve University · US

Funding

Hu proteins as novel splicing regulators in neuronsR01NS049103 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI LOU, HUA · 2004 to 2013
$2.3M
Hu proteins as novel splicing regulators in neuronsR56NS049103 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI LOU, HUA · 2009 to 2009
$353k
NINDS NIH HHS NS-049103-01NINDS NIH HHS R01 NS049103NINDS NIH HHS R56 NS049103
6 · The paper itself

Abstract

Precise and robust regulation of alternative splicing provides cells with an essential means of gene expression control. However, the mechanisms that ensure the tight control of tissue-specific alternative splicing are not well understood. It has been demonstrated that robust regulation often results from the contributions of multiple factors to one particular splicing pathway. We report here a novel strategy used by a single splicing regulator that blocks the formation of two distinct prespliceosome complexes to achieve efficient regulation. Fox-1/Fox-2 proteins, potent regulators of alternative splicing in the heart, skeletal muscle, and brain, repress calcitonin-specific splicing of the calcitonin/CGRP pre-mRNA. Using biochemical analysis, we found that Fox-1/Fox-2 proteins block prespliceosome complex formation at two distinct steps through binding to two functionally important UGCAUG elements. First, Fox-1/Fox-2 proteins bind to the intronic site to inhibit SF1-dependent E' complex formation. Second, these proteins bind to the exonic site to block the transition of E' complex that escaped the control of the intronic site to E complex. These studies provide evidence for the first example of regulated E' complex formation. The two-step repression of presplicing complexes by a single regulator provides a powerful and accurate regulatory strategy.

Indexed as

Base SequenceCalcitoninDNA-Binding ProteinsEnhancer Elements, GeneticExonsHeLa CellsHumansMembrane Cofactor ProteinModels, BiologicalNuclear ProteinsPhosphoproteinsProtein BindingRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA Splice SitesCalcitoninCD46 protein, humanDNA-Binding ProteinsMembrane Cofactor ProteinNuclear ProteinsPhosphoproteinsRBFOX1 protein, humanRBFOX2 protein, humanRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA Splice SitesRNA Splicing FactorsSerine-Arginine Splicing FactorsSF1 protein, humanSplicing Factor U2AFSRSF6 protein, humanTranscription FactorsU2AF2 protein, human

Identifiers

PMID18573872
PMCPMC2519742
OpenAlexW2097779331

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.