Evidence map›Paper›PMID 10648562›Full record

ArticleThe Journal of cell biology2000

An ATP-dependent, Ran-independent mechanism for nuclear import of the U1A and U2B" spliceosome proteins.

M Hetzer, I W Mattaj

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 51 citations in OpenAlex.

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  11. ALADINI482S causes selective failure of nuclear protein import and hypersensitivity to oxidative stress in triple A syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  12. Article
  13. Energetic communication between mitochondria and nucleus directed by catalyzed phosphotransfer.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  14. Article
  15. Disruption of the FG nucleoporin NUP98 causes selective changes in nuclear pore complex stoichiometry and function.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
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

2 authors at 1 institution in 1 country.

M HetzerEuropean Molecular Biology Laboratory (EMBL), D-69117 Heidelberg, Germany.
I W Mattaj
European Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear import of the two uracil-rich small nuclear ribonucleoprotein (U snRNP) components U1A and U2B" is mediated by unusually long and complex nuclear localization signals (NLSs). Here we investigate nuclear import of U1A and U2B" in vitro and demonstrate that it occurs by an active, saturable process. Several lines of evidence suggest that import of the two proteins occurs by an import mechanism different to those characterized previously. No cross competition is seen with a variety of previously studied NLSs. In contrast to import mediated by members of the importin-beta family of nucleocytoplasmic transport receptors, U1A/U2B" import is not inhibited by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant of the GTPase Ran that is incapable of GTP hydrolysis. Adenosine triphosphate is capable of supporting U1A and U2B" import, whereas neither nonhydrolyzable adenosine triphosphate analogues nor GTP can do so. U1A and U2B" import in vitro does not require the addition of soluble cytosolic proteins, but a factor or factors required for U1A and U2B" import remains tightly associated with the nuclear fraction of conventionally permeabilized cells. This activity can be solubilized in the presence of elevated MgCl(2). These data suggest that U1A and U2B" import into the nucleus occurs by a hitherto uncharacterized mechanism.

Indexed as

RNA-Binding ProteinsAdenosine TriphosphateAmino Acid SequenceAutoantigensBiological TransportCell CompartmentationCell Membrane PermeabilityCell NucleusCytosolGuanosine TriphosphateHeLa CellsHumansHydrolysisMolecular Sequence DataMutationNuclear ProteinsAdenosine TriphosphateAutoantigensGuanosine TriphosphateNuclear Proteinsran GTP-Binding ProteinRibonucleoproteins, Small NuclearRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinssnRNP Core ProteinsSNRPB2 protein, humanU1A protein

Identifiers

PMID10648562
PMCPMC2174293
OpenAlexW2145559272

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.