Evidence map›Paper›PMID 26275778›Full record

ArticleNucleic acids research2015

NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins.

Jonathan Bizarro, Maxime Dodré, Alexandra Huttin, Bruno Charpentier, Florence Schlotter, Christiane Branlant, Céline Verheggen, Séverine Massenet, Edouard Bertrand

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.7field-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

43 citing papers in PubMed, 59 citations in OpenAlex.

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  9. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
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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

9 authors at 2 institutions in 1 country.

Jonathan BizarroEquipe labélisée Ligue contre le Cancer, Institut de Génétique Moléculaire de Montpellier, IGMM-UMR 5535 du CNRS-Université de Montpellier, 1919, route de Mende, 34293 Montpellier Cedex 5, France.
Maxime DodréIngénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, avenue de la forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex, France.
Alexandra HuttinIngénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, avenue de la forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex, France.
Bruno CharpentierIngénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, avenue de la forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex, France.
Florence SchlotterIngénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, avenue de la forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex, France.
Christiane BranlantIngénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, avenue de la forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex, France.
Céline VerheggenEquipe labélisée Ligue contre le Cancer, Institut de Génétique Moléculaire de Montpellier, IGMM-UMR 5535 du CNRS-Université de Montpellier, 1919, route de Mende, 34293 Montpellier Cedex 5, France celine.verheggen@igmm.cnrs.fr.
Séverine MassenetIngénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, avenue de la forêt de Haye, BP 184, 54505 Vandoeuvre-les-Nancy Cedex, France severine.massenet@univ-lorraine.fr.
Edouard BertrandEquipe labélisée Ligue contre le Cancer, Institut de Génétique Moléculaire de Montpellier, IGMM-UMR 5535 du CNRS-Université de Montpellier, 1919, route de Mende, 34293 Montpellier Cedex 5, France edouard.bertrand@igmm.cnrs.fr.
Ingénierie Moléculaire et Physiopathologie Articulaire · FRInstitut de Génétique Moléculaire de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Sm proteins are loaded on snRNAs by the SMN complex, but how snRNP-specific proteins are assembled remains poorly characterized. U4 snRNP and box C/D snoRNPs have structural similarities. They both contain the 15.5K and proteins with NOP domains (PRP31 for U4, NOP56/58 for snoRNPs). Biogenesis of box C/D snoRNPs involves NUFIP and the HSP90/R2TP chaperone system and here, we explore the function of this machinery in U4 RNP assembly. We show that yeast Prp31 interacts with several components of the NUFIP/R2TP machinery, and that these interactions are separable from each other. In human cells, PRP31 mutants that fail to stably associate with U4 snRNA still interact with components of the NUFIP/R2TP system, indicating that these interactions precede binding of PRP31 to U4 snRNA. Knock-down of NUFIP leads to mislocalization of PRP31 and decreased association with U4. Moreover, NUFIP is associated with the SMN complex through direct interactions with Gemin3 and Gemin6. Altogether, our data suggest a model in which the NUFIP/R2TP system is connected with the SMN complex and facilitates assembly of U4 snRNP-specific proteins.

Indexed as

Cell LineCoiled BodiesCytoplasmEye ProteinsHeLa CellsHumansMolecular ChaperonesMutagenesis, InsertionalRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRibonucleoprotein, U4-U6 Small NuclearRibosomal ProteinsRNA, Small NuclearSaccharomyces cerevisiae ProteinsSMN Complex ProteinsSpliceosomesEye ProteinsHit1 protein, S cerevisiaeMolecular ChaperonesPRP31 protein, S cerevisiaePRPF31 protein, humanRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRibonucleoprotein, U4-U6 Small NuclearRibosomal ProteinsRNA, Small NuclearRSA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMN Complex ProteinsSnu13 protein, humanU4 small nuclear RNA

Identifiers

PMID26275778
PMCPMC4605303
OpenAlexW2164428568

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.