Evidence map›Paper›PMID 9864357›Full record

ArticleThe Journal of cell biology1998

Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p.

M Marelli, J D Aitchison, R W Wozniak

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

81 citing papers in PubMed, 153 citations in OpenAlex.

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  9. Identification of the NovelG3 (Bethesda, Md.) · 2018
    Article
  10. Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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21 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

3 authors at 1 institution in 1 country.

M MarelliDepartment of Cell Biology, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.
J D Aitchison
R W Wozniak
University of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have identified a specific karyopherin docking complex within the yeast nuclear pore complex (NPC) that contains two novel, structurally related nucleoporins, Nup53p and Nup59p, and the NPC core protein Nup170p. This complex was affinity purified from cells expressing a functional Nup53p-protein A chimera. The localization of Nup53p, Nup59p, and Nup170p within the NPC by immunoelectron microscopy suggests that the Nup53p-containing complex is positioned on both the cytoplasmic and nucleoplasmic faces of the NPC core. In association with the isolated complex, we have also identified the nuclear transport factor Kap121p (Pse1p). Using in vitro binding assays, we showed that each of the nucleoporins interacts with one another. However, the association of Kap121p with the complex is mediated by its interaction with Nup53p. Moreover, Kap121p is the only beta-type karyopherin that binds Nup53p suggesting that Nup53p acts as a specific Kap121p docking site. Kap121p can be released from Nup53p by the GTP bound form of the small GTPase Ran. The physiological relevance of the interaction between Nup53p and Kap121p was further underscored by the observation that NUP53 mutations alter the subcellular distribution of Kap121p and the Kap121p- mediated import of a ribosomal L25 reporter protein. Interestingly, Nup53p is specifically phosphorylated during mitosis. This phenomenon is correlated with a transient decrease in perinuclear-associated Kap121p.

Indexed as

Membrane Transport ProteinsNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceFungal ProteinsGenetic Complementation TestMacromolecular SubstancesMembrane GlycoproteinsMembrane ProteinsMitosisMolecular Sequence DataNuclear EnvelopeNuclear PoreNuclear ProteinsPhosphorylationPorinsASM4 protein, S cerevisiaeFungal ProteinsMacromolecular SubstancesMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNUP170 protein, S cerevisiaeNUP53 protein, S cerevisiaePOM152 protein, S cerevisiaePorinsProtein KinasesPSE1 protein, S cerevisiaeran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID9864357
PMCPMC2175238
OpenAlexW1996364283

What OpenQuestion holds

Textmetadata
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.