Evidence map›Paper›PMID 27882870›Full record

ArticleeLife2016

Large-scale remodeling of a repressed exon ribonucleoprotein to an exon definition complex active for splicing.

Somsakul Pop Wongpalee, Ajay Vashisht, Shalini Sharma, Darryl Chui, James A Wohlschlegel, Douglas L Black

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  4. Condensation of ZFP207 and U1 snRNP promotes spliceosome assembly.Nature structural & molecular biology · 2025
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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

6 authors at 2 institutions in 1 country.

Somsakul Pop WongpaleeDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.
Ajay VashishtDepartment of Biological Chemistry, University of California, Los Angeles, Los Angeles, United States.
Shalini SharmaDepartment of Basic Medical Sciences, University of Arizona, Phoenix, United States.
Darryl ChuiDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.
James A WohlschlegelDepartment of Biological Chemistry, University of California, Los Angeles, Los Angeles, United States.
Douglas L BlackDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.ORCID 0000-0002-2705-8187
University of California, Los Angeles · USUniversity of Arizona · US

Funding

The Regulation of Neuronal Exon SplicingR01GM049662 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLACK, DOUGLAS L · 1998 to 2019
$6.5M
Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
Examining role of splicing factor mutations in myelodysplastic syndrome (PQ11)R21CA170786 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SHARMA, SHALINI · 2012 to 2013
$366k
Howard Hughes Medical InstituteNCI NIH HHS R21 CA170786NIGMS NIH HHS R01 GM049662NIGMS NIH HHS R01 GM089778
6 · The paper itself

Abstract

Polypyrimidine-tract binding protein PTBP1 can repress splicing during the exon definition phase of spliceosome assembly, but the assembly steps leading to an exon definition complex (EDC) and how PTBP1 might modulate them are not clear. We found that PTBP1 binding in the flanking introns allowed normal U2AF and U1 snRNP binding to the target exon splice sites but blocked U2 snRNP assembly in HeLa nuclear extract. Characterizing a purified PTBP1-repressed complex, as well as an active early complex and the final EDC by SILAC-MS, we identified extensive PTBP1-modulated changes in exon RNP composition. The active early complex formed in the absence of PTBP1 proceeded to assemble an EDC with the eviction of hnRNP proteins, the late recruitment of SR proteins, and binding of the U2 snRNP. These results demonstrate that during early stages of splicing, exon RNP complexes are highly dynamic with many proteins failing to bind during PTBP1 arrest.

Indexed as

ExonsRNA SplicingHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansMass SpectrometryPolypyrimidine Tract-Binding ProteinRNA, Small NuclearSpliceosomesSplicing Factor U2AFHeterogeneous-Nuclear RibonucleoproteinsPolypyrimidine Tract-Binding ProteinPTBP1 protein, humanRNA, Small NuclearSplicing Factor U2AFU1 small nuclear RNAU2 small nuclear RNAbiochemistryevolutionary biologygene regulationgenomicshumanribonucleoproteinRNA binding proteinsplicing

Identifiers

PMID27882870
PMCPMC5122456
OpenAlexW2555191339

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.