Evidence map›Paper›PMID 24748666›Full record

ArticleNucleic acids research2014

The crystal structure of the Split End protein SHARP adds a new layer of complexity to proteins containing RNA recognition motifs.

Fabiana Arieti, Caroline Gabus, Margherita Tambalo, Tiphaine Huet, Adam Round, Stéphane Thore

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Article
  8. Getting to the bottom of lncRNA mechanism: structure-function relationships.Mammalian genome : official journal of the International Mammalian Genome Society · 2022
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Mechanistic insights in X-chromosome inactivation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  17. Article
  18. Function by Structure: Spotlights on Xist Long Non-coding RNA.Frontiers in molecular biosciences · 2017
    Review
  19. Article
  20. 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

6 authors at 2 institutions in 2 countries.

Fabiana ArietiDepartment of Molecular Biology, University of Geneva, Geneva 1211, Switzerland.
Caroline GabusDepartment of Molecular Biology, University of Geneva, Geneva 1211, Switzerland.
Margherita TambaloDepartment of Molecular Biology, University of Geneva, Geneva 1211, Switzerland.
Tiphaine HuetDepartment of Molecular Biology, University of Geneva, Geneva 1211, Switzerland.
Adam RoundEuropean Molecular Biology Laboratory, Grenoble Outstation and Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, Grenoble 38042, France.
Stéphane ThoreDepartment of Molecular Biology, University of Geneva, Geneva 1211, Switzerland stephane.thore@unige.ch.
University of Geneva · CHEuropean Molecular Biology Laboratory · FR

Funding

Worldwide Cancer Research 14-0346
6 · The paper itself

Abstract

The Split Ends (SPEN) protein was originally discovered in Drosophila in the late 1990s. Since then, homologous proteins have been identified in eukaryotic species ranging from plants to humans. Every family member contains three predicted RNA recognition motifs (RRMs) in the N-terminal region of the protein. We have determined the crystal structure of the region of the human SPEN homolog that contains these RRMs-the SMRT/HDAC1 Associated Repressor Protein (SHARP), at 2.0 Å resolution. SHARP is a co-regulator of the nuclear receptors. We demonstrate that two of the three RRMs, namely RRM3 and RRM4, interact via a highly conserved interface. Furthermore, we show that the RRM3-RRM4 block is the main platform mediating the stable association with the H12-H13 substructure found in the steroid receptor RNA activator (SRA), a long, non-coding RNA previously shown to play a crucial role in nuclear receptor transcriptional regulation. We determine that SHARP association with SRA relies on both single- and double-stranded RNA sequences. The crystal structure of the SHARP-RRM fragment, together with the associated RNA-binding studies, extend the repertoire of nucleic acid binding properties of RRM domains suggesting a new hypothesis for a better understanding of SPEN protein functions.

Indexed as

Amino Acid MotifsCrystallography, X-RayDNA-Binding ProteinsHomeodomain ProteinsHumansModels, MolecularNuclear ProteinsNucleic Acid ConformationProtein BindingRNARNA-Binding ProteinsDNA-Binding ProteinsHomeodomain ProteinsNuclear ProteinsRNARNA-Binding ProteinsSPEN protein, human

Identifiers

PMID24748666
PMCPMC4041450
OpenAlexW2156541397

What OpenQuestion holds

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LicenceCC BY-NC
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.