Evidence map›Paper›PMID 24795046›Full record

ArticleThe Journal of biological chemistry2014

Cancer-relevant splicing factor CAPERα engages the essential splicing factor SF3b155 in a specific ternary complex.

Sarah Loerch, Alexandre Maucuer, Valérie Manceau, Michael R Green, Clara L Kielkopf

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

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  12. RNA binding proteins in MLL-rearranged leukemia.Experimental hematology & oncology · 2022
    Review
  13. Article
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  16. 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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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.

Sarah LoerchFrom the Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642 and.
Alexandre Maucuerthe Howard Hughes Medical Institute and Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605 alexandre.maucuer@inserm.fr.
Valérie Manceauthe Howard Hughes Medical Institute and Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605.
Michael R Greenthe Howard Hughes Medical Institute and Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605.
Clara L KielkopfFrom the Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642 and clara_kielkopf@urmc.rochester.edu.

Funding

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
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR026501NIGMS NIH HHS R01 GM035490NIGMS NIH HHS R01 GM070503
6 · The paper itself

Abstract

U2AF homology motifs (UHMs) mediate protein-protein interactions with U2AF ligand motifs (ULMs) of pre-mRNA splicing factors. The UHM-containing alternative splicing factor CAPERα regulates splicing of tumor-promoting VEGF isoforms, yet the molecular target of the CAPERα UHM is unknown. Here we present structures of the CAPERα UHM bound to a representative SF3b155 ULM at 1.7 Å resolution and, for comparison, in the absence of ligand at 2.2 Å resolution. The prototypical UHM/ULM interactions authenticate CAPERα as a bona fide member of the UHM family of proteins. We identify SF3b155 as the relevant ULM-containing partner of full-length CAPERα in human cell extracts. Isothermal titration calorimetry comparisons of the purified CAPERα UHM binding known ULM-containing proteins demonstrate that high affinity interactions depend on the presence of an intact, intrinsically unstructured SF3b155 domain containing seven ULM-like motifs. The interplay among bound CAPERα molecules gives rise to the appearance of two high affinity sites in the SF3b155 ULM-containing domain. In conjunction with the previously identified, UHM/ULM-mediated complexes of U2AF(65) and SPF45 with SF3b155, this work demonstrates the capacity of SF3b155 to offer a platform for coordinated recruitment of UHM-containing splicing factors.

Indexed as

Amino Acid MotifsHEK293 CellsHumansNeoplasm ProteinsNuclear ProteinsPhosphoproteinsProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsHCC1 autoantigenNeoplasm ProteinsNuclear ProteinsPhosphoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSF3B1 protein, humanCrystal StructureGene RegulationProtein DomainProtein-Protein InteractionProtein Structure and FoldingRNA Splicing

Identifiers

PMID24795046
PMCPMC4067167

What OpenQuestion holds

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Registered trials

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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.