Evidence map›Paper›PMID 11352933›Full record

ArticleThe Journal of cell biology2001

A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope.

M Marelli, C P Lusk, H Chan, J D Aitchison, R W Wozniak

Open access · bronzeAbstract read
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 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

78 citing papers in PubMed, 134 citations in OpenAlex.

  1. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
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  6. Synthesis of CInternational journal of molecular sciences · 2022
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  9. Article
  10. Review
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  14. Review
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  17. Nucleoporins in cardiovascular disease.Journal of molecular and cellular cardiology · 2020
    Review
  18. Article
  19. Article
  20. Article

18 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 2 institutions in 2 countries.

M MarelliDepartment of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
C P Lusk
H Chan
J D Aitchison
R W Wozniak
University of Alberta · CAInstitute for Systems Biology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear pore complex (NPC) is a multicomponent structure containing a subset of proteins that bind nuclear transport factors or karyopherins and mediate their movement across the nuclear envelope. By altering the expression of a single nucleoporin gene, NUP53, we showed that the overproduction of Nup53p altered nuclear transport and had a profound effect on the structure of the nuclear membrane. Strikingly, conventional and immunoelectron microscopy analysis revealed that excess Nup53p entered the nucleus and associated with the nuclear membrane. Here, Nup53p induced the formation of intranuclear, tubular membranes that later formed flattened, double membrane lamellae structurally similar to the nuclear envelope. Like the nuclear envelope, the intranuclear double membrane lamellae enclosed a defined cisterna that was interrupted by pores but, unlike the nuclear envelope pores, they lacked NPCs. Consistent with this observation, we detected only two NPC proteins, the pore membrane proteins Pom152p and Ndc1p, in association with these membrane structures. Thus, these pores likely represent an intermediate in NPC assembly. We also demonstrated that the targeting of excess Nup53p to the NPC and its specific association with intranuclear membranes were dependent on the karyopherin Kap121p and the nucleoporin Nup170p. At the nuclear envelope, the abilities of Nup53p to associate with the membrane and drive membrane proliferation were dependent on a COOH-terminal segment containing a potential amphipathic alpha-helix. The implications of these results with regards to the biogenesis of the nuclear envelope are discussed.

Indexed as

Membrane Transport ProteinsNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsActive Transport, Cell NucleusFungal ProteinsGene Expression Regulation, FungalMembrane GlycoproteinsMembrane ProteinsMicroscopy, ElectronNuclear EnvelopeNuclear PoreNuclear ProteinsPlasmidsPorinsProtein Structure, SecondaryProtein Structure, TertiaryFungal ProteinsMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNDC1 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNUP170 protein, S cerevisiaeNUP53 protein, S cerevisiaePOM152 protein, S cerevisiaePorinsPSE1 protein, S cerevisiaeReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID11352933
PMCPMC2192385
OpenAlexW1972848630

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.