Evidence map›Paper›PMID 33367824›Full record

ArticleNucleic acids research2021

NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis.

Yoann Abel, Ana C F Paiva, Jonathan Bizarro, Marie-Eve Chagot, Paulo E Santo, Marie-Cécile Robert, Marc Quinternet, Franck Vandermoere, Pedro M F Sousa, Philippe Fort and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

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  12. Genenames.org: the HGNC resources in 2023.Nucleic acids research · 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

15 authors at 2 institutions in 2 countries.

Yoann AbelIGMM, CNRS, Univ Montpellier, Montpellier, France.
Ana C F PaivaiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, 2781-901, Portugal.
Jonathan BizarroIGMM, CNRS, Univ Montpellier, Montpellier, France.
Marie-Eve ChagotUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France.
Paulo E SantoiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, 2781-901, Portugal.
Marie-Cécile RobertIGMM, CNRS, Univ Montpellier, Montpellier, France.
Marc QuinternetUniversité de Lorraine, CNRS, INSERM, IBSLor, Biophysics and Structural Biology Core Facility, F-54000, Nancy, France.
Franck VandermoereIGF, CNRS, INSERM, Univ Montpellier, Montpellier, France.
Pedro M F SousaiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, 2781-901, Portugal.
Philippe FortCRBM, CNRS, Univ Montpellier, Montpellier, France.
Bruno CharpentierUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France.
Xavier ManivalUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France.
Tiago M BandeirasiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, 2781-901, Portugal.
Edouard BertrandIGMM, CNRS, Univ Montpellier, Montpellier, France.
Céline VerheggenIGMM, CNRS, Univ Montpellier, Montpellier, France.
Centre National de la Recherche Scientifique · FRInstituto de Biologia Experimental e Tecnológica · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PAQosome is a large complex composed of the HSP90/R2TP chaperone and a prefoldin-like module. It promotes the biogenesis of cellular machineries but it is unclear how it discriminates closely related client proteins. Among the main PAQosome clients are C/D snoRNPs and in particular their core protein NOP58. Using NOP58 mutants and proteomic experiments, we identify different assembly intermediates and show that C12ORF45, which we rename NOPCHAP1, acts as a bridge between NOP58 and PAQosome. NOPCHAP1 makes direct physical interactions with the CC-NOP domain of NOP58 and domain II of RUVBL1/2 AAA+ ATPases. Interestingly, NOPCHAP1 interaction with RUVBL1/2 is disrupted upon ATP binding. Moreover, while it robustly binds both yeast and human NOP58, it makes little interactions with NOP56 and PRPF31, two other closely related CC-NOP proteins. Expression of NOP58, but not NOP56 or PRPF31, is decreased in NOPCHAP1 KO cells. We propose that NOPCHAP1 is a client-loading PAQosome cofactor that selects NOP58 to promote box C/D snoRNP assembly.

Indexed as

Adenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesEye ProteinsGene Knockout TechniquesGenes, ReporterHeLa CellsHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesMultiprotein ComplexesNuclear ProteinsProtein DomainsProtein Interaction MappingProteomicsAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesEye ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesMultiprotein ComplexesNOP56 protein, humanNOP58 protein, humanNOP58 protein, S cerevisiaeNuclear ProteinsPRPF31 protein, humanRecombinant Fusion ProteinsRibonucleoproteins, Small NucleolarRUVBL1 protein, humanRUVBL2 protein, humanSaccharomyces cerevisiae Proteins

Identifiers

PMID33367824
PMCPMC7826282
OpenAlexW3112687631

What OpenQuestion holds

Textmetadata
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.