Evidence map›Paper›PMID 24240281›Full record

ArticleNature2014

Coupled GTPase and remodelling ATPase activities form a checkpoint for ribosome export.

Yoshitaka Matsuo, Sander Granneman, Matthias Thoms, Rizos-Georgios Manikas, David Tollervey, Ed Hurt

Open access · greenAbstract read
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

102 citing papers in PubMed, 149 citations in OpenAlex.

  1. RiboScreenBiomedicines · 2026
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42 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Yoshitaka MatsuoBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany.
Sander Granneman *Wellcome Trust Centre for Cell Biology, The University of Edinburgh, Edinburgh UK.
Matthias Thoms *Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany.
Rizos-Georgios ManikasBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany.
David TollerveyWellcome Trust Centre for Cell Biology, The University of Edinburgh, Edinburgh UK.
Ed HurtBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany.
Heidelberg University · DEUniversity of Edinburgh · GBWellcome Centre for Cell Biology · GB

Funding

Wellcome Trust 077248Wellcome Trust 092076
6 · The paper itself

Abstract

Eukaryotic ribosomes are assembled by a complex pathway that extends from the nucleolus to the cytoplasm and is powered by many energy-consuming enzymes. Nuclear export is a key, irreversible step in pre-ribosome maturation, but mechanisms underlying the timely acquisition of export competence remain poorly understood. Here we show that a conserved Saccharomyces cerevisiae GTPase Nug2 (also known as Nog2, and as NGP-1, GNL2 or nucleostemin 2 in human) has a key role in the timing of export competence. Nug2 binds the inter-subunit face of maturing, nucleoplasmic pre-60S particles, and the location clashes with the position of Nmd3, a key pre-60S export adaptor. Nug2 and Nmd3 are not present on the same pre-60S particles, with Nug2 binding before Nmd3. Depletion of Nug2 causes premature Nmd3 binding to the pre-60S particles, whereas mutations in the G-domain of Nug2 block Nmd3 recruitment, resulting in severe 60S export defects. Two pre-60S remodelling factors, the Rea1 ATPase and its co-substrate Rsa4, are present on Nug2-associated particles, and both show synthetic lethal interactions with nug2 mutants. Release of Nug2 from pre-60S particles requires both its K(+)-dependent GTPase activity and the remodelling ATPase activity of Rea1. We conclude that Nug2 is a regulatory GTPase that monitors pre-60S maturation, with release from its placeholder site linked to recruitment of the nuclear export machinery.

Indexed as

Adenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCell NucleusCytoplasmGenes, LethalGTP PhosphohydrolasesModels, MolecularMutationPotassiumProtein BindingProtein Structure, TertiaryRibosomal ProteinsRibosomesRibosome Subunits, Large, EukaryoticRNA-Binding ProteinsSaccharomyces cerevisiaeAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesGTP PhosphohydrolasesMDN1 protein, S cerevisiaeNMD3 protein, S cerevisiaeNOG2 protein, S cerevisiaePotassiumRibosomal ProteinsRNA-Binding ProteinsRsa4 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID24240281
PMCPMC3880858
OpenAlexW2130966021

What OpenQuestion holds

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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.