Evidence map›Paper›PMID 22064476›Full record

ArticleMolecular and cellular biology2012

A U1-U2 snRNP interaction network during intron definition.

Wei Shao, Hyun-Soo Kim, Yang Cao, Yong-Zhen Xu, Charles C Query

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 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.8field-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

53 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Condensation of ZFP207 and U1 snRNP promotes spliceosome assembly.Nature structural & molecular biology · 2025
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  5. Review
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  8. Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  19. Article
  20. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    Review
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

5 authors at 3 institutions in 2 countries.

Wei ShaoKey Laboratory of Insect Developmental and Evolutionary Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
Hyun-Soo Kim
Yang Cao
Yong-Zhen Xu
Charles C Query
Albert Einstein College of Medicine · USCenter for Excellence in Molecular Plant Sciences · CNShanghai Institutes for Biological Sciences · CN

Funding

PROTEIN RNA REARRANGEMENTS IN THE SPLICEOSOMER01GM057829 · NIGMS · YESHIVA UNIVERSITY · PI QUERY, CHARLES C · 1999 to 2025
$11.4M
NIGMS NIH HHS GM57829NIGMS NIH HHS R01 GM057829
6 · The paper itself

Abstract

The assembly of prespliceosomes is responsible for selection of intron sites for splicing. U1 and U2 snRNPs recognize 5' splice sites and branch sites, respectively; although there is information regarding the composition of these complexes, little is known about interaction among the components or between the two snRNPs. Here we describe the protein network of interactions linking U1 and U2 snRNPs with the ATPase Prp5, important for branch site recognition and fidelity during the first steps of the reaction, using fission yeast Schizosaccharomyces pombe. The U1 snRNP core protein U1A binds to a novel SR-like protein, Rsd1, which has homologs implicated in transcription. Rsd1 also contacts S. pombe Prp5 (SpPrp5), mediated by SR-like domains in both proteins. SpPrp5 then contacts U2 snRNP through SF3b, mediated by a conserved DPLD motif in Prp5. We show that mutations in this motif have consequences not only in vitro (defects in prespliceosome formation) but also in vivo, yielding intron retention and exon skipping defects in fission yeast and altered intron recognition in budding yeast Saccharomyces cerevisiae, indicating that the U1-U2 network provides critical, evolutionarily conserved contacts during intron definition.

Indexed as

IntronsProtein Interaction MappingAdenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceConserved SequenceMutationPhosphoric Monoester HydrolasesProtein BindingProtein Interaction Domains and MotifsRibonucleoprotein, U2 Small NuclearRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsAdenosine TriphosphatasesPhosphoric Monoester HydrolasesPRP5 protein, S pombeRibonucleoprotein, U2 Small NuclearRNA, Small NuclearSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsU1 small nuclear RNA

Identifiers

PMID22064476
PMCPMC3255776
OpenAlexW1965463749

What OpenQuestion holds

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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.