Evidence map›Paper›PMID 11739405›Full record

ArticleThe Journal of cell biology2001

Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex.

P E Gleizes, J Noaillac-Depeyre, I Léger-Silvestre, F Teulières, J Y Dauxois, D Pommet, M C Azum-Gelade, N Gas

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In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 56 citations in OpenAlex.

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  6. Cryo-ET reveals the macromolecular reorganization ofProceedings of the National Academy of Sciences of the United States of America · 2018
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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

8 authors at 2 institutions in 1 country.

P E GleizesLaboratoire de Biologie Moléculaire Eucaryote, Centre Nationale de la Recherche Scientifique and Université Paul Sabatier, 31062 Toulouse cedex, France. gleizes@ibcg.biotoul.fr
J Noaillac-Depeyre
I Léger-Silvestre
F Teulières
J Y Dauxois
D Pommet
M C Azum-Gelade
N Gas
Université Toulouse III - Paul Sabatier · FRÉcole Nationale de la Statistique et de l'Analyse de l'Information · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To study the nuclear export of preribosomes, ribosomal RNAs were detected by in situ hybridization using fluorescence and EM, in the yeast Saccharomyces cerevisiae. In wild-type cells, semiquantitative analysis shows that the distributions of pre-40S and pre-60S particles in the nucleolus and the nucleoplasm are distinct, indicating uncoordinated transport of the two subunits within the nucleus. In cells defective for the activity of the GTPase Gsp1p/Ran, ribosomal precursors accumulate in the whole nucleus. This phenotype is reproduced with pre-60S particles in cells defective in pre-rRNA processing, whereas pre-40S particles only accumulate in the nucleolus, suggesting a tight control of the exit of the small subunit from the nucleolus. Examination of nucleoporin mutants reveals that preribosome nuclear export requires the Nup82p-Nup159p-Nsp1p complex. In contrast, mutations in the nucleoporins forming the Nup84p complex yield very mild or no nuclear accumulation of preribosome. Interestingly, domains of Nup159p required for mRNP trafficking are not necessary for preribosome export. Furthermore, the RNA helicase Dbp5p and the protein Gle1p, which interact with Nup159p and are involved in mRNP trafficking, are dispensable for ribosomal transport. Thus, the Nup82p-Nup159p-Nsp1p nucleoporin complex is part of the nuclear export pathways of preribosomes and mRNPs, but with distinct functions in these two processes.

Indexed as

Calcium-Binding ProteinsSaccharomyces cerevisiae ProteinsActive Transport, Cell NucleusCytoplasmFungal ProteinsIn Situ HybridizationMicroscopy, ElectronMutagenesisNuclear Pore Complex ProteinsNuclear ProteinsRibonucleoproteinsRibosomesRNA, RibosomalSaccharomyces cerevisiaeCalcium-Binding ProteinsFungal Proteinsmessenger ribonucleoproteinNSP1 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNUP159 protein, S cerevisiaeNUP82 protein, S cerevisiaeRibonucleoproteinsRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID11739405
PMCPMC2150900
OpenAlexW2085883257

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LicenceCC BY-NC-SA
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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.