Evidence map›Paper›PMID 12773398›Full record

ArticleThe EMBO journal2003

Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates.

Christopher R Trotta, Elsebet Lund, Lawrence Kahan, Arlen W Johnson, James E Dahlberg

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

74 citing papers in PubMed, 129 citations in OpenAlex.

  1. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
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14 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

5 authors at 1 institution in 1 country.

Christopher R TrottaDepartment of Biomolecular Chemistry, University of Wisconsin Medical School, 1300 University Avenue, Madison, WI 53706, USA.
Elsebet Lund
Lawrence Kahan
Arlen W Johnson
James E Dahlberg
University of Wisconsin–Madison · US

Funding

MRNA DEGRADATION AND TRANSLATION CONTROL IN YEASTR01GM053655 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSON, ARLEN W · 1995 to 2017
$5.1M
RNAS AND PROTEINS BETWEEN THE NUCLEUS AND CYTOPLASMR37GM030220 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI DAHLBERG, JAMES E · 1998 to 2005
$3.1M
STRUCTURE, ORGANIZATION, AND EXPRESSION OF SNRNA GENESR01GM030220 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI DAHLBERG, JAMES E · 1985 to 1997
–
NIGMS NIH HHS GM30220NIGMS NIH HHS GM53655NIGMS NIH HHS R01 GM053655NIGMS NIH HHS R37 GM030220
6 · The paper itself

Abstract

60S and 40S ribosomal subunits are assembled in the nucleolus and exported from the nucleus to the cytoplasm independently of each other. We show that in vertebrate cells, transport of both subunits requires the export receptor CRM1 and Ran.GTP. Export of 60S subunits is coupled with that of the nucleo- cytoplasmic shuttling protein NMD3. Human NMD3 (hNMD3) contains a CRM-1-dependent leucine-rich nuclear export signal (NES) and a complex, dispersed nuclear localization signal (NLS), the basic region of which is also required for nucleolar accumulation. When present in Xenopus oocytes, both wild-type and export-defective mutant hNMD3 proteins bind to newly made nuclear 60S pre-export particles at a late step of subunit maturation. The export-defective hNMD3, but not the wild-type protein, inhibits export of 60S subunits from oocyte nuclei. These results indicate that the NES mutant protein competes with endogenous wild-type frog NMD3 for binding to nascent 60S subunits, thereby preventing their export. We propose that NMD3 acts as an adaptor for CRM1-Ran.GTP-mediated 60S subunit export, by a mechanism that is conserved from vertebrates to yeast.

Indexed as

Receptors, Cytoplasmic and NuclearActive Transport, Cell NucleusAmino Acid SequenceAnimalsBinding, CompetitiveConserved SequenceExportin 1 ProteinFemaleHeLa CellsHumansIn Vitro TechniquesKaryopherinsMolecular Sequence DataMutationNuclear Localization SignalsOocytesExportin 1 ProteinKaryopherinsNMD3 protein, humanNuclear Localization Signalsran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRNA-Binding Proteins

Identifiers

PMID12773398
PMCPMC156746
OpenAlexW1971653995

What OpenQuestion holds

Textmetadata
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.