Evidence map›Paper›PMID 23273425›Full record

ArticleStructure (London, England : 1993)2013

Structure of phosphorylated SF1 bound to U2AF⁶⁵ in an essential splicing factor complex.

Wenhua Wang, Alexandre Maucuer, Ankit Gupta, Valérie Manceau, Karen R Thickman, William J Bauer, Scott D Kennedy, Joseph E Wedekind, Michael R Green, Clara L Kielkopf

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

24 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Role ofFrontiers in plant science · 2020
    Article
  12. U2AFEMBO reports · 2019
    Article
  13. Article
  14. International journal of molecular sciences · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shift.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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

10 authors at 3 institutions in 2 countries.

Wenhua WangCenter for RNA Biology and Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.
Alexandre Maucuer
Ankit Gupta
Valérie Manceau
Karen R Thickman
William J Bauer
Scott D Kennedy
Joseph E Wedekind
Michael R Green
Clara L Kielkopf
University of Rochester · USHoward Hughes Medical Institute · USJohns Hopkins University · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
Molecular Recognition During Pre-mRNA SplicingR01GM070503 · NIGMS · UNIVERSITY OF ROCHESTER · PI KIELKOPF, CLARA · 2004 to 2025
$7.9M
SPLICING OF MRNA PRECURSORSR01GM035490 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GREEN, MICHAEL R · 1985 to 2021
$4.7M
A shared macromolecular X-ray diffraction system in RochesterS10RR026501 · NCRR · UNIVERSITY OF ROCHESTER · PI WEDEKIND, JOSEPH E · 2010 to 2010
$478k
NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NCRR NIH HHS P41 RR001646NCRR NIH HHS RR01646NCRR NIH HHS S10 RR026501NIGMS NIH HHS R01 GM035490NIGMS NIH HHS R01 GM070503
6 · The paper itself

Abstract

The essential splicing factors U2AF⁶⁵ and SF1 cooperatively bind consensus sequences at the 3' end of introns. Phosphorylation of SF1 on a highly conserved "SPSP" motif enhances its interaction with U2AF⁶⁵ and the pre-mRNA. Here, we reveal that phosphorylation induces essential conformational changes in SF1 and in the SF1/U2AF⁶⁵/3' splice site complex. Crystal structures of the phosphorylated (P)SF1 domain bound to the C-terminal domain of U2AF⁶⁵ at 2.29 Å resolution and of the unphosphorylated SF1 domain at 2.48 Å resolution demonstrate that phosphorylation induces a disorder-to-order transition within a previously unknown SF1/U2AF⁶⁵ interface. We find by small-angle X-ray scattering that the local folding of the SPSP motif transduces into global conformational changes in the nearly full-length (P)SF1/U2AF⁶⁵/3' splice site assembly. We further determine that SPSP phosphorylation and the SF1/U2AF⁶⁵ interface are essential in vivo. These results offer a structural prototype for phosphorylation-dependent control of pre-mRNA splicing factors.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsBase SequenceCell ProliferationCrystallography, X-RayDNA-Binding ProteinsHEK293 CellsHeLa CellsHumansHydrogen BondingMiceModels, MolecularMolecular Sequence DataNIH 3T3 CellsNuclear ProteinsDNA-Binding ProteinsNuclear ProteinsRibonucleoproteinsRNA Splice SitesRNA Splicing FactorsSF1 protein, humanSplicing Factor U2AFTranscription FactorsU2AF2 protein, humanZrsr1 protein, mouse

Identifiers

PMID23273425
PMCPMC3570649
OpenAlexW2037778125

What OpenQuestion holds

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LicenceTDM
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.