Evidence map›Paper›PMID 18268104›Full record

ArticleThe Journal of cell biology2008

The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery.

Séverine Boulon, Nathalie Marmier-Gourrier, Bérengère Pradet-Balade, Laurence Wurth, Céline Verheggen, Beáta E Jády, Benjamin Rothé, Christina Pescia, Marie-Cécile Robert, Tamás Kiss and 6 more

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In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
9.0field-weighted citation impact, top 1% 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

130 citing papers in PubMed, 227 citations in OpenAlex.

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70 more citing papers are in PubMed but not listed here.

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

16 authors at 6 institutions in 1 country.

Séverine BoulonInstitute of Molecular Genetics of Montpellier, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5535, Montpellier Cedex 5, France.
Nathalie Marmier-Gourrier
Bérengère Pradet-Balade
Laurence Wurth
Céline Verheggen
Beáta E Jády
Benjamin Rothé
Christina Pescia
Marie-Cécile Robert
Tamás Kiss
Barbara Bardoni
Alain Krol
Christiane Branlant
Christine Allmang
Edouard Bertrand
Bruno Charpentier
Institut de Génétique Moléculaire de Montpellier · FRCentre National de la Recherche Scientifique · FRUniversité Toulouse III - Paul Sabatier · FRArchitecture et Réactivité de l'arN · FRInstitut de génétique et de biologie moléculaire et cellulaire · FRUniversité de Lorraine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA-binding proteins of the L7Ae family are at the heart of many essential ribonucleoproteins (RNPs), including box C/D and H/ACA small nucleolar RNPs, U4 small nuclear RNP, telomerase, and messenger RNPs coding for selenoproteins. In this study, we show that Nufip and its yeast homologue Rsa1 are key components of the machinery that assembles these RNPs. We observed that Rsa1 and Nufip bind several L7Ae proteins and tether them to other core proteins in the immature particles. Surprisingly, Rsa1 and Nufip also link assembling RNPs with the AAA + adenosine triphosphatases hRvb1 and hRvb2 and with the Hsp90 chaperone through two conserved adaptors, Tah1/hSpagh and Pih1. Inhibition of Hsp90 in human cells prevents the accumulation of U3, U4, and telomerase RNAs and decreases the levels of newly synthesized hNop58, hNHP2, 15.5K, and SBP2. Thus, Hsp90 may control the folding of these proteins during the formation of new RNPs. This suggests that Hsp90 functions as a master regulator of cell proliferation by allowing simultaneous control of cell signaling and cell growth.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsCell ProliferationConserved SequenceDNA-Binding ProteinsDNA HelicasesEvolution, MolecularHeterogeneous-Nuclear Ribonucleoprotein LHSP90 Heat-Shock ProteinsMolecular ChaperonesNuclear ProteinsProtein BindingProtein FoldingRibosomal ProteinsRNA-Binding ProteinsSaccharomyces cerevisiaeAdenosine TriphosphatasesCell Cycle ProteinsDNA-Binding ProteinsDNA HelicasesHeterogeneous-Nuclear Ribonucleoprotein LHSP90 Heat-Shock ProteinsMolecular ChaperonesNuclear ProteinsNUFIP1 protein, humanPIH1 protein, S cerevisiaeRibosomal ProteinsRNA-Binding ProteinsRSA1 protein, S cerevisiaeRVB1 protein, S cerevisiaeRVB2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTAH11 protein, S cerevisiaeTranscription Factors

Identifiers

PMID18268104
PMCPMC2234240
OpenAlexW2153084026

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.