Evidence map›Paper›PMID 20498018›Full record

ArticleThe Journal of cell biology2010

Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution.

Anne Chadrin, Barbara Hess, Mabel San Roman, Xavier Gatti, Bérangère Lombard, Damarys Loew, Yves Barral, Benoit Palancade, Valérie Doye

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

63 citing papers in PubMed, 101 citations in OpenAlex.

  1. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  3. Article
  4. Review
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  9. ER-phagy requires the assembly of actin at sites of contact between the cortical ER and endocytic pits.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  17. Article
  18. Review
  19. Review
  20. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review

3 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

9 authors at 4 institutions in 2 countries.

Anne ChadrinInstitut Jacques Monod, UMR 7592, Centre National de la Recherche Scientifique/Université Paris Diderot, 75013 Paris, France.
Barbara Hess
Mabel San Roman
Xavier Gatti
Bérangère Lombard
Damarys Loew
Yves Barral
Benoit Palancade
Valérie Doye
Université Paris Cité · FRETH Zurich · CHInstitut Curie · FRInstitut Jacques Monod · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biogenesis of nuclear pore complexes (NPCs) represents a paradigm for the assembly of high-complexity macromolecular structures. So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope. Here, we describe the identification and functional characterization of Pom33, a novel transmembrane protein dynamically associated with budding yeast NPCs. Pom33 becomes critical for yeast viability in the absence of a functional Nup84 complex or Ndc1 interaction network, which are two core NPC subcomplexes, and associates with the reticulon Rtn1. Moreover, POM33 loss of function impairs NPC distribution, a readout for a subset of genes required for pore biogenesis, including members of the Nup84 complex and RTN1. Consistently, we show that Pom33 is required for normal NPC density in the daughter nucleus and for proper NPC biogenesis and/or stability in the absence of Nup170. We hypothesize that, by modifying or stabilizing the nuclear envelope-NPC interface, Pom33 may contribute to proper distribution and/or efficient assembly of nuclear pores.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceCell ProliferationEndoplasmic ReticulumMembrane ProteinsMolecular Sequence DataNuclear PoreNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsPhylogenyProtein BindingRecombinant Fusion ProteinsRepressor ProteinsRibonuclease IIIRNA-Binding ProteinsRNA, MessengerMembrane ProteinsMIG1 protein, S cerevisiaeNAB2 protein, S cerevisiaeNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsNUP133 protein, S cerevisiaeNUP157 protein, S cerevisiaeNUP170 protein, S cerevisiaeNUP84 protein, S cerevisiaePom33 protein, S cerevisiaeRecombinant Fusion ProteinsRepressor ProteinsRibonuclease IIIRNA-Binding ProteinsRNA, MessengerRNT1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID20498018
PMCPMC2878943
OpenAlexW1985802550

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.